{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:06:41Z","timestamp":1790726801706,"version":"4.1.0"},"reference-count":234,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2023,5,7]],"date-time":"2023-05-07T00:00:00Z","timestamp":1683417600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000780","name":"European Union\u2019s Horizon 2020 research and innovation programme","doi-asserted-by":"publisher","award":["H2020-MSCA-ITN-2018-812661"],"award-info":[{"award-number":["H2020-MSCA-ITN-2018-812661"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000780","name":"European Union\u2019s Horizon 2020 research and innovation programme","doi-asserted-by":"publisher","award":["890610"],"award-info":[{"award-number":["890610"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004955","name":"Austrian Research Promotion Agency (FFG)","doi-asserted-by":"publisher","award":["H2020-MSCA-ITN-2018-812661"],"award-info":[{"award-number":["H2020-MSCA-ITN-2018-812661"]}],"id":[{"id":"10.13039\/501100004955","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004955","name":"Austrian Research Promotion Agency (FFG)","doi-asserted-by":"publisher","award":["890610"],"award-info":[{"award-number":["890610"]}],"id":[{"id":"10.13039\/501100004955","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Lipopolysaccharide (LPS), also referred to as endotoxin, is the major component of Gram-negative bacteria\u2019s outer cell wall. It is one of the main types of pathogen-associated molecular patterns (PAMPs) that are known to elicit severe immune reactions in the event of a pathogen trespassing the epithelial barrier and reaching the bloodstream. Associated symptoms include fever and septic shock, which in severe cases, might even lead to death. Thus, the detection of LPS in medical devices and injectable pharmaceuticals is of utmost importance. However, the term LPS does not describe one single molecule but a diverse class of molecules sharing one common feature: their characteristic chemical structure. Each bacterial species has its own pool of LPS molecules varying in their chemical composition and enabling the aggregation into different supramolecular structures upon release from the bacterial cell wall. As this heterogeneity has consequences for bioassays, we aim to examine the great variability of LPS molecules and their potential to form various supramolecular structures. Furthermore, we describe current LPS quantification methods and the LPS-dependent inflammatory pathway and show how LPS heterogeneity can affect them. With the intent of overcoming these challenges and moving towards a universal approach for targeting LPS, we review current studies concerning LPS-specific binders. Finally, we give perspectives for LPS research and the use of LPS-binding molecules.<\/jats:p>","DOI":"10.3390\/ijms24098395","type":"journal-article","created":{"date-parts":[[2023,5,8]],"date-time":"2023-05-08T03:34:53Z","timestamp":1683516893000},"page":"8395","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":85,"title":["Heterogeneity of Lipopolysaccharide as Source of Variability in Bioassays and LPS-Binding Proteins as Remedy"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8745-829X","authenticated-orcid":false,"given":"Alexandra C.","family":"Fux","sequence":"first","affiliation":[{"name":"Division of Allergy & Immunology, Department of Biosciences & Medical Biology, Paris Lodron University of Salzburg (PLUS), Hellbrunnerstra\u00dfe 34, 5020 Salzburg, Austria"},{"name":"Chemical Biology Department, R&D Reagents, Miltenyi Biotec B.V. & Co. KG, Friedrich-Ebert-Stra\u00dfe 68, 51429 Bergisch Gladbach, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1013-585X","authenticated-orcid":false,"given":"Cristiane","family":"Casonato Melo","sequence":"additional","affiliation":[{"name":"Division of Allergy & Immunology, Department of Biosciences & Medical Biology, Paris Lodron University of Salzburg (PLUS), Hellbrunnerstra\u00dfe 34, 5020 Salzburg, Austria"},{"name":"Chemical Biology Department, R&D Reagents, Miltenyi Biotec B.V. & Co. KG, Friedrich-Ebert-Stra\u00dfe 68, 51429 Bergisch Gladbach, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9470-3337","authenticated-orcid":false,"given":"Sara","family":"Michelini","sequence":"additional","affiliation":[{"name":"Biotechnical Faculty, Department of Biology, University of Ljubljana, Ve\u010dna pot 111, 1000 Ljubljana, Slovenia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6283-5199","authenticated-orcid":false,"given":"Benjamin J.","family":"Swartzwelter","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Pathology, 1601 Campus Delivery, Colorado State University, Fort Collins, CO 80523, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8020-9311","authenticated-orcid":false,"given":"Andreas","family":"Neusch","sequence":"additional","affiliation":[{"name":"Experimental Medical Physics, Heinrich-Heine University D\u00fcsseldorf, Universit\u00e4tsstra\u00dfe 1, 40225 D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9830-2733","authenticated-orcid":false,"given":"Paola","family":"Italiani","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Cell Biology, Consiglio Nazionale delle Ricerche (CNR), Via P. Castellino 111, 80131 Naples, Italy"},{"name":"Stazione Zoologica Anton Dohrn (SZN), Villa Comunale, 80121 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5416-085X","authenticated-orcid":false,"given":"Martin","family":"Himly","sequence":"additional","affiliation":[{"name":"Division of Allergy & Immunology, Department of Biosciences & Medical Biology, Paris Lodron University of Salzburg (PLUS), Hellbrunnerstra\u00dfe 34, 5020 Salzburg, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,5,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1038\/s41579-022-00779-w","article-title":"Soil Microbiomes and One Health","volume":"21","author":"Banerjee","year":"2023","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"818.e1","DOI":"10.1016\/j.cell.2020.01.018","article-title":"SnapShot: Microbial Extremophiles","volume":"180","author":"Schmid","year":"2020","journal-title":"Cell"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"4055","DOI":"10.1002\/ejoc.201700113","article-title":"Gram-Negative Extremophile Lipopolysaccharides: Promising Source of Inspiration for a New Generation of Endotoxin Antagonists","volume":"2017","author":"Billod","year":"2017","journal-title":"Eur. J. Org. Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"780","DOI":"10.3389\/fmicb.2019.00780","article-title":"Living at the Extremes: Extremophiles and the Limits of Life in a Planetary Context","volume":"10","author":"Merino","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1096\/fasebj.8.2.8119492","article-title":"Bacterial Endotoxin: Molecular Relationships of Structure to Activity and Function","volume":"8","author":"Rietschel","year":"1994","journal-title":"FASEB J."},{"key":"ref_6","first-page":"450","article-title":"Panum\u2019s Studies on \u201cPutrid Poison\u201d 1856","volume":"53","author":"Kolmos","year":"2006","journal-title":"Dan. Med. Bull."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1007\/BF02284303","article-title":"Untersuchungen \u00dcber Das Choleragift","volume":"11","author":"Pfeiffer","year":"1892","journal-title":"Z. F\u00fcr Hyg. Und Infekt."},{"key":"ref_8","unstructured":"(2023, April 12). ICH Guideline Q4B\u2014Annex 14 to Note for Evaluation and Recommendation of Pharmacopoeial Texts for Use in the ICH Regions on Bacterial Endotoxins Tests. Available online: https:\/\/www.ema.europa.eu\/en\/documents\/scientific-guideline\/draft-ich-guideline-q4b-annex-14-note-evaluation-recommendation-pharmacopoeial-texts-use-ich-regions_en.pdf."},{"key":"ref_9","unstructured":"Stromberg, L.R., Mendez, H.M., and Mukundan, H. (2017). Escherichia coli\u2014Recent Advances on Physiology, Pathogenesis and Biotechnological Applications, InTech."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1111\/j.1574-6976.2006.00016.x","article-title":"The Structures of Escherichia coli O-Polysaccharide Antigens","volume":"30","author":"Stenutz","year":"2006","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1111\/j.1365-2958.2004.03987.x","article-title":"Lipopolysaccharide O Antigen Status of Yersinia enterocolitica O:8 Is Essential for Virulence and Absence of O Antigen Affects the Expression of Other Yersinia Virulence Factors","volume":"52","author":"Bengoechea","year":"2004","journal-title":"Mol. Microbiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2008","DOI":"10.1046\/j.1432-1327.2000.01204.x","article-title":"Biological Activities of Lipopolysaccharides Are Determined by the Shape of Their Lipid A Portion","volume":"267","author":"Schromm","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1177\/1753425909106436","article-title":"Lipopolysaccharide Biosynthesis in Pseudomonas aeruginosa","volume":"15","author":"King","year":"2009","journal-title":"Innate Immun."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1146\/annurev.biochem.71.110601.135414","article-title":"Lipopolysaccharide Endotoxins","volume":"71","author":"Raetz","year":"2002","journal-title":"Annu. Rev. Biochem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1093\/femsre\/fuz028","article-title":"Structure and Genetics of Escherichia Coli O Antigens","volume":"44","author":"Liu","year":"2020","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1111\/j.1469-0691.2007.01876.x","article-title":"Role of Structural Variations of Polysaccharide Antigens in the Pathogenicity of Gram-Negative Bacteria","volume":"14","year":"2008","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1111\/febs.12104","article-title":"Intact Rough- and Smooth-form Lipopolysaccharides from Escherichia Coli Separated by Preparative Gel Electrophoresis Exhibit Differential Biologic Activity in Human Macrophages","volume":"280","author":"Pupo","year":"2013","journal-title":"FEBS J."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1111\/j.1432-1033.1981.tb06241.x","article-title":"Structural Studies on the Hexose Region of the Core in Lipopolysaccharides from Enterobacteriaceae","volume":"115","author":"Jansson","year":"1981","journal-title":"Eur. J. Biochem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1128\/IAI.68.3.1116-1124.2000","article-title":"Distribution of Core Oligosaccharide Types in Lipopolysaccharides from Escherichia coli","volume":"68","author":"Amor","year":"2000","journal-title":"Infect. Immun."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1111\/j.1432-1033.1989.tb14677.x","article-title":"Structural Analysis of the Nontoxic Lipid A of Rhodobacter capsulatus 37b4","volume":"180","author":"Krauss","year":"1989","journal-title":"Eur. J. Biochem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1111\/j.1432-1033.1994.tb18616.x","article-title":"Characterization of the Lipopolysaccharide of Moraxella catarrhalis","volume":"220","author":"Masoud","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1007\/BF00249110","article-title":"The Structure of the Lipid A Component of Sphaerotilus natans","volume":"156","author":"Masoud","year":"1991","journal-title":"Arch. Microbiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"11222","DOI":"10.1074\/jbc.275.15.11222","article-title":"Characterization of a Novel Lipid A Containing D-Galacturonic Acid That Replaces Phosphate Residues","volume":"275","author":"Lindner","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2922","DOI":"10.1002\/chem.200902390","article-title":"The Structure of a Novel Neutral Lipid A from the Lipopolysaccharide of Bradyrhizobium elkanii Containing Three Mannose Units in the Backbone","volume":"16","author":"Komaniecka","year":"2010","journal-title":"Chem. Eur. J."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1094\/MPMI-11-16-0230-R","article-title":"The Lipopolysaccharide Lipid A Long-Chain Fatty Acid Is Important for Rhizobium leguminosarum Growth and Stress Adaptation in Free-Living and Nodule Environments","volume":"30","author":"Bourassa","year":"2017","journal-title":"Mol. Plant-Microbe Interact."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Pither, M.D., Mantova, G., Scaglione, E., Pagliuca, C., Colicchio, R., Vitiello, M., Chernikov, O.V., Hua, K.-F., Kokoulin, M.S., and Silipo, A. (2021). The Unusual Lipid A Structure and Immunoinhibitory Activity of LPS from Marine Bacteria Echinicola Pacifica KMM 6172T and Echinicola Vietnamensis KMM 6221T. Microorganisms, 9.","DOI":"10.3390\/microorganisms9122552"},{"key":"ref_27","first-page":"113","article-title":"The Lipopolysaccaride of Legionella pneumophila Serogroup 1 (Strain Philadelphia1): Chemical structure and biological significance","volume":"1","author":"Zaehringer","year":"1995","journal-title":"Prog. Clin. Biol. Res."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1177\/09680519010070011001","article-title":"Bacterial Modification of LPS and Resistance to Antimicrobial Peptides","volume":"7","author":"Gunn","year":"2001","journal-title":"J. Endotoxin Res."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1146\/annurev.biochem.76.010307.145803","article-title":"Lipid A Modification Systems in Gram-Negative Bacteria","volume":"76","author":"Raetz","year":"2007","journal-title":"Annu. Rev. Biochem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/1475-2859-5-13","article-title":"Brucella Spp. Noncanonical LPS: Structure, Biosynthesis, and Interaction with Host Immune System","volume":"5","author":"Cardoso","year":"2006","journal-title":"Microb. Cell Fact."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1126\/science.274.5289.980","article-title":"Antibacterial Agents That Inhibit Lipid A Biosynthesis","volume":"274","author":"Onishi","year":"1996","journal-title":"Science"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"21203","DOI":"10.1074\/jbc.M111.239475","article-title":"The Lipid A from Vibrio fischeri Lipopolysaccharide","volume":"286","author":"Phillips","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Irvine, K.L., Gangloff, M., Walsh, C.M., Spring, D.R., Gay, N.J., and Bryant, C.E. (2014). Identification of Key Residues That Confer Rhodobacter sphaeroides LPS Activity at Horse TLR4\/MD-2. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0098776"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1194\/jlr.M800454-JLR200","article-title":"Structural Characterization of Bordetella parapertussis Lipid A","volume":"50","author":"Novikov","year":"2009","journal-title":"J. Lipid Res."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"30917","DOI":"10.1039\/D0RA05463A","article-title":"Mass Spectrometric Analysis of Lipid A Obtained from the Lipopolysaccharide of Pasteurella multocida","volume":"10","author":"Tawab","year":"2020","journal-title":"RSC Adv."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"69","DOI":"10.4052\/tigg.14.69","article-title":"Chemical Structure of Lipid A\u2014The Primary Immunomodulatory Center of Bacterial Lipopolysaccharide","volume":"14","author":"Christian","year":"2002","journal-title":"Trends Glycosci. Glycotechnol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"01019","DOI":"10.1051\/e3sconf\/202132201019","article-title":"Effects of Fatty Acid from Deep-Sea Microorganisms on Lipid Bilayer Membrane Fluidity under High Pressure: Comparison of Branched-Chain and Polyunsaturated Fatty Acid","volume":"322","author":"Miura","year":"2021","journal-title":"E3S Web Conf."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"184","DOI":"10.3390\/md11010184","article-title":"The Lipid A from the Haloalkaliphilic Bacterium Salinivibrio Sharmensis Strain BAGT","volume":"11","author":"Carillo","year":"2013","journal-title":"Mar. Drugs"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Di Lorenzo, F., Crisafi, F., La Cono, V., Yakimov, M.M., Molinaro, A., and Silipo, A. (2020). The Structure of the Lipid A of Gram-Negative Cold-Adapted Bacteria Isolated from Antarctic Environments. Mar. Drugs, 18.","DOI":"10.3390\/md18120592"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"9677","DOI":"10.1074\/jbc.274.14.9677","article-title":"Effect of Cold Shock on Lipid A Biosynthesis in Escherichia coli","volume":"274","author":"Carty","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"4092","DOI":"10.1128\/IAI.70.8.4092-4098.2002","article-title":"Modification of the Structure and Activity of Lipid A in Yersinia pestis Lipopolysaccharide by Growth Temperature","volume":"70","author":"Kawahara","year":"2002","journal-title":"Infect. Immun."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1007\/s10719-022-10076-6","article-title":"Structural Determination of the Lipid A from the Deep-Sea Bacterium Zunongwangia profunda SM-A87: A Small-Scale Approach","volume":"39","author":"Pither","year":"2022","journal-title":"Glycoconj. J."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1086\/521367","article-title":"Unique Lipid A Modifications in Pseudomonas aeruginosa Isolated from the Airways of Patients with Cystic Fibrosis","volume":"196","author":"Ernst","year":"2007","journal-title":"J. Infect. Dis."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1111\/mmi.14365","article-title":"Acidic pH Promotes Lipopolysaccharide Modification and Alters Colonization in a Bacteria\u2013Animal Mutualism","volume":"112","author":"Schwartzman","year":"2019","journal-title":"Mol. Microbiol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1111\/j.1365-2958.2004.04409.x","article-title":"Role of Mg2+ and pH in the Modification of Salmonella Lipid A after Endocytosis by Macrophage Tumour Cells","volume":"55","author":"Gibbons","year":"2005","journal-title":"Mol. Microbiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3743","DOI":"10.1128\/AAC.00256-11","article-title":"The PmrCAB Operon Mediates Polymyxin Resistance in Acinetobacter baumannii ATCC 17978 and Clinical Isolates through Phosphoethanolamine Modification of Lipid A","volume":"55","author":"Arroyo","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1111\/j.1432-1033.1991.tb16244.x","article-title":"Investigation of the Structure of Lipid A from Actinobacillus actinomycetemcomitans Strain Y4 and Human Clinical Isolate PO 1021-7","volume":"200","author":"Masoud","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"10023","DOI":"10.1002\/anie.202012374","article-title":"Lipopolysaccharide from Gut-Associated Lymphoid-Tissue-Resident Alcaligenes faecalis: Complete Structure Determination and Chemical Synthesis of Its Lipid A","volume":"60","author":"Shimoyama","year":"2021","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1111\/j.1432-1033.1989.tb14945.x","article-title":"Structural Characterization of the Lipid A Component of Bacteroides fragilis Strain NCTC 9343 Lipopolysaccharide","volume":"183","author":"Weintraub","year":"1989","journal-title":"Eur. J. Biochem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1021\/acscentsci.0c00791","article-title":"Pairing Bacteroides vulgatus LPS Structure with Its Immunomodulatory Effects on Human Cellular Models","volume":"6","author":"Pither","year":"2020","journal-title":"ACS Cent. Sci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"34221","DOI":"10.1038\/srep34221","article-title":"Bartonella quintana Lipopolysaccharide (LPS): Structure and Characteristics of a Potent TLR4 Antagonist for in-Vitro and in-Vivo Applications","volume":"6","author":"Heinbockel","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1177\/1753425909347400","article-title":"The Lipid A of Burkholderia multivorans C1576 Smooth-Type Lipopolysaccharide and Its pro-Inflammatory Activity in a Cystic Fibrosis Airways Model","volume":"16","author":"Cescutti","year":"2010","journal-title":"Innate Immun."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"5160","DOI":"10.1073\/pnas.0913451107","article-title":"A Link between the Assembly of Flagella and Lipooligosaccharide of the Gram-Negative Bacterium Campylobacter jejuni","volume":"107","author":"Cullen","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"16819","DOI":"10.1074\/jbc.274.24.16819","article-title":"Structural Analysis of the Lipopolysaccharide from Chlamydia trachomatis Serotype L2","volume":"274","author":"Rund","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/1476-069X-5-7","article-title":"Cyanobacterial Lipopolysaccharides and Human Health\u2014A Review","volume":"5","author":"Stewart","year":"2006","journal-title":"Environ. Health"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"4701","DOI":"10.3390\/md13084701","article-title":"Temperature-Dependence of Lipid a Acyl Structure in Psychrobacter Cryohalolentis and Arctic Isolates of Colwellia hornerae and Colwellia piezophila","volume":"13","author":"Sweet","year":"2015","journal-title":"Mar. Drugs"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"S103","DOI":"10.1194\/jlr.R800060-JLR200","article-title":"Discovery of New Biosynthetic Pathways: The Lipid A Story","volume":"50","author":"Raetz","year":"2009","journal-title":"J. Lipid Res."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"5340","DOI":"10.1128\/IAI.72.9.5340-5348.2004","article-title":"Novel Modification of Lipid A of Francisella tularensis","volume":"72","author":"Phillips","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"3277","DOI":"10.1128\/IAI.02011-05","article-title":"Basis for the Failure of Francisella tularensis Lipopolysaccharide to Prime Human Polymorphonuclear Leukocytes","volume":"74","author":"Barker","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1002\/cbic.202000751","article-title":"Structure of the O-Antigen and the Lipid A from the Lipopolysaccharide of Fusobacterium nucleatum ATCC 51191","volume":"22","author":"Lamprinaki","year":"2021","journal-title":"ChemBioChem"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1111\/j.1432-1033.1988.tb14397.x","article-title":"Chemical Structure of the Lipopolysaccharide Haemophilus influenzae Strain I-69 Rd-\/B+","volume":"177","author":"Helander","year":"1988","journal-title":"Eur. J. Biochem."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Di Lorenzo, F., Palmigiano, A., Paciello, I., Pallach, M., Garozzo, D., Bernardini, M.-L., La Cono, V., Yakimov, M.M., Molinaro, A., and Silipo, A. (2017). The Deep-Sea Polyextremophile Halobacteroides lacunaris TB21 Rough-Type LPS: Structure and Inhibitory Activity towards Toxic LPS. Mar. Drugs, 15.","DOI":"10.3390\/md15070201"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1177\/09680519050110030401","article-title":"Remodeling of Helicobacter pylori Lipopolysaccharide","volume":"11","author":"Tran","year":"2005","journal-title":"J. Endotoxin Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1007\/s00284-016-1117-6","article-title":"Identification of Two Genes Encoding for the Late Acyltransferases of Lipid A in Klebsiella pneumoniae","volume":"73","author":"Li","year":"2016","journal-title":"Curr. Microbiol."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Black, I.M., Heiss, C., Jain, M., Muszy\u0144ski, A., Carlson, R.W., Gabriel, D.W., and Azadi, P. (2021). Structure of Lipopolysaccharide from Liberibacter crescens Is Low Molecular Weight and Offers Insight into Candidatus Liberibacter Biology. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222011240"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2895","DOI":"10.1111\/j.1432-1033.2004.04212.x","article-title":"Detailed Structure of Lipid A Isolated from Lipopolysaccharide from the Marine Proteobacterium Marinomonas vaga ATCC 27119T","volume":"271","author":"Krasikova","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Hassan, F., Ren, D., Zhang, W., Merkel, T.J., and Gu, X.-X. (2012). Moraxella Catarrhalis Activates Murine Macrophages through Multiple Toll Like Receptors and Has Reduced Clearance in Lungs from TLR4 Mutant Mice. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0037610"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1128\/JB.00558-09","article-title":"Functional Characterization of Lpt3 and Lpt6, the Inner-Core Lipooligosaccharide Phosphoethanolamine Transferases from Neisseria meningitidis","volume":"192","author":"Wenzel","year":"2010","journal-title":"J. Bacteriol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1128\/IAI.69.3.1477-1482.2001","article-title":"Signaling by Toll-like Receptor 2 and 4 Agonists Results in Differential Gene Expression in Murine Macrophages","volume":"69","author":"Hirschfeld","year":"2001","journal-title":"Infect. Immun."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1111\/j.1432-1033.1983.tb07789.x","article-title":"Chemical Structure of the Lipid A Component of the Lipopolysaccharide from a Proteus mirabilis Re-Mutant","volume":"22","author":"Sidorczyk","year":"1983","journal-title":"Eur. J. Biochem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"475153","DOI":"10.1155\/2012\/475153","article-title":"Molecular Characterization of Lipopolysaccharide Binding to Human \u03b1-1-Acid Glycoprotein","volume":"2012","author":"Huang","year":"2012","journal-title":"J. Lipids"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"4126","DOI":"10.3390\/md12074126","article-title":"Endotoxin Structures in the Psychrophiles Psychromonas marina and Psychrobacter cryohalolentis Contain Distinctive Acyl Features","volume":"12","author":"Sweet","year":"2014","journal-title":"Mar. Drugs"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1051\/ocl\/2020025","article-title":"Lipopolysaccharides: Structure, Function and Bacterial Identification","volume":"27","author":"Caroff","year":"2020","journal-title":"OCL"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1038\/s41586-021-03566-4","article-title":"Ubiquitylation of Lipopolysaccharide by RNF213 during Bacterial Infection","volume":"594","author":"Otten","year":"2021","journal-title":"Nature"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.molimm.2019.03.003","article-title":"Structural Variants of Salmonella typhimurium Lipopolysaccharide Induce Less Dimerization of TLR4\/MD-2 and Reduced pro-Inflammatory Cytokine Production in Human Monocytes","volume":"111","author":"Gunn","year":"2019","journal-title":"Mol. Immunol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1440","DOI":"10.1099\/jmm.0.47327-0","article-title":"Chemical Structure and Immunobiological Activity of Lipid A from Serratia marcescens LPS","volume":"56","author":"Makimura","year":"2007","journal-title":"J. Med. Microbiol."},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Barrau, C., Di Lorenzo, F., Menes, R.J., Lanzetta, R., Molinaro, A., and Silipo, A. (2018). The Structure of the Lipid a from the Halophilic Bacterium Spiribacter salinus M19-40T. Mar. Drugs, 16.","DOI":"10.3390\/md16040124"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"e02283-14","DOI":"10.1128\/mBio.02283-14","article-title":"The Vibrio cholerae VprA-VprB Two-Component System Controls Virulence through Endotoxin Modification","volume":"5","author":"Herrera","year":"2014","journal-title":"MBio"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"22984","DOI":"10.1073\/pnas.1917504117","article-title":"Early Evolutionary Loss of the Lipid A Modifying Enzyme PagP Resulting in Innate Immune Evasion in Yersinia pestis","volume":"117","author":"Chandler","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_80","first-page":"388","article-title":"Methods of Endotoxin Removal from Biological Preparations: A Review","volume":"10","author":"Lopes","year":"2007","journal-title":"J. Pharm. Pharm. Sci."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1002\/cbic.200390020","article-title":"Evaluation of Lipopolysaccharide Aggregation by Light Scattering Spectroscopy","volume":"4","author":"Santos","year":"2003","journal-title":"ChemBioChem"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"6811","DOI":"10.1016\/j.biomaterials.2005.04.063","article-title":"Endotoxin: The Uninvited Guest","volume":"26","author":"Gorbet","year":"2005","journal-title":"Biomaterials"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.colsurfb.2006.06.007","article-title":"Aggregation Behavior and Size of Lipopolysaccharide from Escherichia coli O55:B5","volume":"53","author":"Bergstrand","year":"2006","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.colsurfb.2007.10.002","article-title":"ATR-FTIR Study of Lipopolysaccharides at Mineral Surfaces","volume":"62","author":"Parikh","year":"2008","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.aca.2005.09.008","article-title":"Determination of Critical Micelle Concentrations and Aggregation Numbers by Fluorescence Correlation Spectroscopy: Aggregation of a Lipopolysaccharide","volume":"556","author":"Yu","year":"2006","journal-title":"Anal. Chim. Acta"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1128\/jb.92.5.1493-1509.1966","article-title":"Reaction of Endotoxin and Surfactants","volume":"92","author":"Ribi","year":"1966","journal-title":"J. Bacteriol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1021\/la503267k","article-title":"Characterization of the Aggregates Formed by Various Bacterial Lipopolysaccharides in Solution and upon Interaction with Antimicrobial Peptides","volume":"31","author":"Bello","year":"2015","journal-title":"Langmuir"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"2104211","DOI":"10.1002\/smll.202104211","article-title":"Human Antimicrobial Peptide Triggered Colloidal Transformations in Bacteria Membrane Lipopolysaccharides","volume":"18","author":"Hong","year":"2022","journal-title":"Small"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.colsurfb.2006.12.014","article-title":"Infrared Spectroscopy Studies of Cation Effects on Lipopolysaccharides in Aqueous Solution","volume":"55","author":"Parikh","year":"2007","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"44750","DOI":"10.1038\/srep44750","article-title":"Biological Activity of Masked Endotoxin","volume":"7","author":"Schwarz","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1006\/abio.1998.2655","article-title":"Proteinase K Digestion of Proteins Improves Detection of Bacterial Endotoxins by the Limulus Amebocyte Lysate Assay: Application for Endotoxin Removal from Cationic Proteins","volume":"259","author":"Petsch","year":"1998","journal-title":"Anal. Biochem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"25078","DOI":"10.1016\/S0021-9258(17)31501-6","article-title":"Hemoglobin, a Newly Recognized Lipopolysaccharide (LPS)-Binding Protein That Enhances LPS Biological Activity","volume":"269","author":"Kaca","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1177\/1753425911422723","article-title":"Endotoxin\u00b7albumin Complexes Transfer Endotoxin Monomers to MD-2 Resulting in Activation of TLR4","volume":"18","author":"Esparza","year":"2012","journal-title":"Innate Immun."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.bbamem.2015.11.007","article-title":"The Influence of Rough Lipopolysaccharide Structure on Molecular Interactions with Mammalian Antimicrobial Peptides","volume":"1858","author":"Bello","year":"2016","journal-title":"BBA\u2014Biomembr."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2085","DOI":"10.1126\/science.282.5396.2085","article-title":"Defective LPS Signaling in C3H\/HeJ and C57BL\/10ScCr Mice: Mutations in TLR4 Gene","volume":"282","author":"Poltorak","year":"1998","journal-title":"Science"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"3749","DOI":"10.4049\/jimmunol.162.7.3749","article-title":"Cutting Edge: Toll-Like Receptor 4 (TLR4)-Deficient Mice Are Hyporesponsive to Lipopolysaccharide: Evidence for TLR4 as the Lps Gene Product","volume":"162","author":"Hoshino","year":"1999","journal-title":"J. Immunol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"461","DOI":"10.3389\/fimmu.2014.00461","article-title":"Toll-Like Receptor Signaling Pathways","volume":"5","author":"Kawasaki","year":"2014","journal-title":"Front. Immunol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"2045860","DOI":"10.1155\/2020\/2045860","article-title":"Toll-Like Receptors in Natural Killer Cells and Their Application for Immunotherapy","volume":"2020","author":"Noh","year":"2020","journal-title":"J. Immunol. Res."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1866","DOI":"10.1016\/S0016-5085(03)00403-7","article-title":"Intestinal Myofibroblasts in Innate Immune Responses of the Intestine","volume":"124","author":"Otte","year":"2003","journal-title":"Gastroenterology"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1038\/ni809","article-title":"Essential Role of MD-2 in LPS Responsiveness and TLR4 Distribution","volume":"3","author":"Nagai","year":"2002","journal-title":"Nat. Immunol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1038\/nature07830","article-title":"The Structural Basis of Lipopolysaccharide Recognition by the TLR4\u2013MD-2 Complex","volume":"458","author":"Park","year":"2009","journal-title":"Nature"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"7648","DOI":"10.1039\/D0NR09153G","article-title":"Gold Nanoparticles (AuNPs) Impair LPS-Driven Immune Responses by Promoting a Tolerogenic-like Dendritic Cell Phenotype with Altered Endosomal Structures","volume":"13","author":"Michelini","year":"2021","journal-title":"Nanoscale"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1016\/j.bbalip.2017.01.004","article-title":"Lipid A Structural Modifications in Extreme Conditions and Identification of Unique Modifying Enzymes to Define the Toll-like Receptor 4 Structure-Activity Relationship","volume":"1862","author":"Scott","year":"2017","journal-title":"BBA\u2014Mol. Cell Biol. Lipids"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1038\/ni1569","article-title":"TRAM Couples Endocytosis of Toll-like Receptor 4 to the Induction of Interferon-\u03b2","volume":"9","author":"Kagan","year":"2008","journal-title":"Nat. Immunol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1111\/j.1365-2567.2004.01976.x","article-title":"Signal Transduction by the Lipopolysaccharide Receptor, Toll-like Receptor-4","volume":"113","year":"2004","journal-title":"Immunology"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1016\/j.cell.2016.04.015","article-title":"Bacterial Outer Membrane Vesicles Mediate Cytosolic Localization of LPS and Caspase-11 Activation","volume":"165","author":"Vanaja","year":"2016","journal-title":"Cell"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/JLB.3MIR1118-434R","article-title":"Detecting Lipopolysaccharide in the Cytosol of Mammalian Cells: Lessons from MD-2\/TLR4","volume":"106","author":"Barker","year":"2019","journal-title":"J. Leukoc. Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.3389\/fmicb.2017.01053","article-title":"Outer Membrane Vesicles (OMVs) of Gram-Negative Bacteria: A Perspective Update","volume":"8","author":"Jan","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"585146","DOI":"10.3389\/fimmu.2020.585146","article-title":"Lipopolysaccharide Recognition in the Crossroads of TLR4 and Caspase-4\/11 Mediated Inflammatory Pathways","volume":"11","author":"Zamyatina","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1016\/j.immuni.2018.08.016","article-title":"The Endotoxin Delivery Protein HMGB1 Mediates Caspase-11-Dependent Lethality in Sepsis","volume":"49","author":"Deng","year":"2018","journal-title":"Immunity"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"484","DOI":"10.3389\/fimmu.2020.00484","article-title":"Targeting Inflammation Driven by HMGB1","volume":"11","author":"Yang","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"3063","DOI":"10.4049\/jimmunol.2000373","article-title":"Function and Regulation of Noncanonical Caspase-4\/5\/11 Inflammasome","volume":"204","author":"Matikainen","year":"2020","journal-title":"J. Immunol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"3125","DOI":"10.1038\/ncomms4125","article-title":"TRPA1 Channels Mediate Acute Neurogenic Inflammation and Pain Produced by Bacterial Endotoxins","volume":"5","author":"Meseguer","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Mazgaeen, L., and Gurung, P. (2020). Recent Advances in Lipopolysaccharide Recognition Systems. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21020379"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"29731","DOI":"10.1074\/jbc.M000184200","article-title":"CD14-Dependent Lipopolysaccharide-Induced \u03b2-Defensin-2 Expression in Human Tracheobronchial Epithelium","volume":"275","author":"Becker","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0008-8749(03)00006-6","article-title":"Lactoferrin Down-Regulates the LPS-Induced Cytokine Production in Monocytic Cells via NF-\u03baB","volume":"220","author":"Ohlsson","year":"2002","journal-title":"Cell. Immunol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1111\/j.1939-1676.1990.tb03119.x","article-title":"Endotoxic Shock","volume":"4","author":"Hardie","year":"1990","journal-title":"J. Vet. Intern. Med."},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Duerr, C.U., Zenk, S.F., Chassin, C., Pott, J., G\u00fctle, D., Hensel, M., and Hornef, M.W. (2009). O-Antigen Delays Lipopolysaccharide Recognition and Impairs Antibacterial Host Defense in Murine Intestinal Epithelial Cells. PLOS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000567"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1038\/s41467-018-02861-5","article-title":"Lipopolysaccharide O-Antigen Delays Plant Innate Immune Recognition of Xylella fastidiosa","volume":"9","author":"Rapicavoli","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"16045","DOI":"10.1038\/nrdp.2016.45","article-title":"Sepsis and Septic Shock","volume":"2","author":"Hotchkiss","year":"2016","journal-title":"Nat. Rev. Dis. Prim."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"8144","DOI":"10.1128\/IAI.73.12.8144-8152.2005","article-title":"Comparative Toll-Like Receptor 4-Mediated Innate Host Defense to Bordetella Infection","volume":"73","author":"Mann","year":"2005","journal-title":"Infect. Immun."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.ejpb.2022.10.006","article-title":"Lipopolysaccharide Structure and the Phenomenon of Low Endotoxin Recovery","volume":"180","author":"Gorman","year":"2022","journal-title":"Eur. J. Pharm. Biopharm."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1086\/515176","article-title":"Lipopolysaccharide Structure Influences the Macrophage Response via CD14-Independent and CD14-Dependent Pathways","volume":"28","author":"Gangloff","year":"1999","journal-title":"Clin. Infect. Dis."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"8695","DOI":"10.1074\/jbc.M109.075127","article-title":"MD-2-Mediated Ionic Interactions between Lipid A and TLR4 Are Essential for Receptor Activation","volume":"285","author":"Meng","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1038\/s41467-017-02682-y","article-title":"Human Caspase-4 Detects Tetra-Acylated LPS and Cytosolic Francisella and Functions Differently from Murine Caspase-11","volume":"9","author":"Lagrange","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Arenas, J., Pupo, E., Phielix, C., David, D., Zariri, A., Zamyatina, A., Tommassen, J., and van der Ley, P. (2020). Shortening the Lipid A Acyl Chains of Bordetella Pertussis Enables Depletion of Lipopolysaccharide Endotoxic Activity. Vaccines, 8.","DOI":"10.3390\/vaccines8040594"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"3125","DOI":"10.1128\/iai.63.8.3125-3130.1995","article-title":"The Inflammatory Cytokine Response to Chlamydia Trachomatis Infection Is Endotoxin Mediated","volume":"63","author":"Ingalls","year":"1995","journal-title":"Infect. Immun."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"3011","DOI":"10.1128\/iai.65.8.3011-3016.1997","article-title":"Diphosphoryl Lipid A from Rhodobacter sphaeroides Inhibits Complexes That Form in Vitro between Lipopolysaccharide (LPS)-Binding Protein, Soluble CD14, and Spectrally Pure LPS","volume":"65","author":"Jarvis","year":"1997","journal-title":"Infect. Immun."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.3389\/fimmu.2018.01888","article-title":"Bradyrhizobium Lipid A: Immunological Properties and Molecular Basis of Its Binding to the Myeloid Differentiation Protein-2\/Toll-Like Receptor 4 Complex","volume":"9","author":"Billod","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"5484","DOI":"10.1074\/jbc.M509193200","article-title":"Structural Regions of MD-2 That Determine the Agonist-Antagonist Activity of Lipid IVa","volume":"281","author":"Muroi","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1128\/CVI.00336-09","article-title":"Immunomodulatory Effects of Yersinia Pestis Lipopolysaccharides on Human Macrophages","volume":"17","author":"Matsuura","year":"2010","journal-title":"Clin. Vaccine Immunol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1111\/j.1365-2958.2004.04059.x","article-title":"Variation in Lipid A Structure in the Pathogenic Yersiniae","volume":"52","author":"Rebeil","year":"2004","journal-title":"Mol. Microbiol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3389\/fcimb.2013.00003","article-title":"Recognition of Lipid A Variants by the TLR4-MD-2 Receptor Complex","volume":"3","author":"Maeshima","year":"2013","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"6446","DOI":"10.1128\/IAI.72.11.6446-6454.2004","article-title":"Intact Gram-Negative Helicobacter pylori, Helicobacter felis, and Helicobacter hepaticus Bacteria Activate Innate Immunity via Toll-Like Receptor 2 but Not Toll-Like Receptor 4","volume":"72","author":"Mandell","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/S1471-4906(01)02169-X","article-title":"Does the Shape of Lipid A Determine the Interaction of LPS with Toll-like Receptors?","volume":"23","author":"Netea","year":"2002","journal-title":"Trends Immunol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2920","DOI":"10.1128\/JB.01868-07","article-title":"Identification of a Second Lipopolysaccharide in Porphyromonas Gingivalis W50","volume":"190","author":"Rangarajan","year":"2008","journal-title":"J. Bacteriol."},{"key":"ref_137","unstructured":"(2023, April 14). EDQM European Pharmacopoeia to Put an End to the Rabbit Pyrogen Test. Available online: https:\/\/www.edqm.eu\/en\/-\/european-pharmacopoeia-to-put-an-end-to-the-rabbit-pyrogen-test."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"104491","DOI":"10.1016\/j.dci.2022.104491","article-title":"New Insights into the Hemolymph Coagulation Cascade of Horseshoe Crabs Initiated by Autocatalytic Activation of a Lipopolysaccharide-Sensitive Zymogen","volume":"135","author":"Kawabata","year":"2022","journal-title":"Dev. Comp. Immunol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"3962","DOI":"10.1074\/jbc.M609198200","article-title":"A Structural Perspective on the Interaction between Lipopolysaccharide and Factor C, a Receptor Involved in Recognition of Gram-Negative Bacteria","volume":"282","author":"Koshiba","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_140","unstructured":"Williams, K.L. (2019). Discovery and Early Development of the Limulus Test, Springer International Publishing."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.jcis.2019.05.013","article-title":"Understanding Lipopolysaccharide Aggregation and Its Influence on Activation of Factor C","volume":"552","author":"Wang","year":"2019","journal-title":"J. Colloid Interface Sci."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0049-3848(92)90124-S","article-title":"Molecular Mechanism of Hemolymph Clotting System in Limulus","volume":"68","author":"Iwanaga","year":"1992","journal-title":"Thromb. Res."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/oxfordjournals.jbchem.a021894","article-title":"New Types of Clotting Factors and Defense Molecules Found in Horseshoe Crab Hemolymph: Their Structures and Functions","volume":"123","author":"Iwanaga","year":"1998","journal-title":"J. Biochem."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1385\/1-59259-216-3:3","article-title":"Assay of Endotoxin by Limulus Amebocyte Lysate","volume":"Volume 36","author":"Ketchum","year":"2000","journal-title":"Septic Shock Methods and Protocols"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1177\/096805199400100407","article-title":"Limulus Amebocyte Lysate (LAL) Detection of Endotoxin in Human Blood","volume":"1","author":"Novitsky","year":"1994","journal-title":"J. Endotoxin Res."},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Sandle, T. (2016). Pharmaceutical Microbiology, Elsevier.","DOI":"10.1016\/B978-0-08-100022-9.00001-3"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1159\/000214260","article-title":"Chromogenic Substrates for Horseshoe Crab Clotting Enzyme","volume":"7","author":"Iwanaga","year":"1978","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"e23470","DOI":"10.1002\/bip.23470","article-title":"Low Endotoxin Recovery and Its Impact on Endotoxin Detection","volume":"112","author":"Cao","year":"2021","journal-title":"Biopolymers"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"2477","DOI":"10.1128\/jcm.29.11.2477-2483.1991","article-title":"Sensitivity of Limulus Amebocyte Lysate (LAL) to LAL-Reactive Glucans","volume":"29","author":"Roslansky","year":"1991","journal-title":"J. Clin. Microbiol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.biologicals.2016.04.012","article-title":"Masking of Endotoxin in Surfactant Samples: Effects on Limulus-Based Detection Systems","volume":"44","author":"Reich","year":"2016","journal-title":"Biologicals"},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Reich, J., Weyer, F.A., Tamura, H., Nagaoka, I., and Motschmann, H. (2019). Low Endotoxin Recovery\u2014Masking of Naturally Occuring Endotoxin. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20040838"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1128\/CMR.8.2.268","article-title":"Endotoxemia: Methods of Detection and Clinical Correlates","volume":"8","author":"Hurley","year":"1995","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"iii","DOI":"10.1038\/nmeth.f.350","article-title":"EndoLISA\u00ae: A Novel and Reliable Method for Endotoxin Detection","volume":"8","author":"Grallert","year":"2011","journal-title":"Nat. Methods"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"106241","DOI":"10.1016\/j.mimet.2021.106241","article-title":"Effect of Different Sample Treatment Methods on Low Endotoxin Recovery Phenomenon","volume":"186","author":"Bu","year":"2021","journal-title":"J. Microbiol. Methods"},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Maloney, T., Phelan, R., and Simmons, N. (2018). Saving the Horseshoe Crab: A Synthetic Alternative to Horseshoe Crab Blood for Endotoxin Detection. PLoS Biol., 16.","DOI":"10.7287\/peerj.preprints.26922v1"},{"key":"ref_156","first-page":"321","article-title":"A Recombinant Factor C Procedure for the Detection of Gram-Negative Bacterial Endotoxin","volume":"36","author":"Loverock","year":"2010","journal-title":"United States Pharmacop. Conv.-Pharmacop. Forum"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1007\/s10856-013-5136-6","article-title":"Highly Sensitive Pyrogen Detection on Medical Devices by the Monocyte Activation Test","volume":"25","author":"Stang","year":"2014","journal-title":"J. Mater. Sci. Mater. Med."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1016\/0019-2791(76)90181-6","article-title":"Binding of Polymyxin B to the Lipid A Portion of Bacterial Lipopolysaccharides","volume":"13","author":"Morrison","year":"1976","journal-title":"Immunochemistry"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1039\/D1FD00036E","article-title":"Interactions of Polymyxin B with Lipopolysaccharide-Containing Membranes","volume":"232","author":"Goode","year":"2021","journal-title":"Faraday Discuss."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/0003-2697(92)90017-2","article-title":"Polymyxin B-Horseradish Peroxidase Conjugates as Tools in Endotoxin Research","volume":"207","author":"Appelmelk","year":"1992","journal-title":"Anal. Biochem."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1111\/j.1423-0410.1987.tb04893.x","article-title":"Endotoxin-Polymyxin Complexes in an Improved Enzyme-Linked Immunosorbent Assay for IgG Antibodies in Blood Donor Sera to Gram-Negative Endotoxin Core Glycolipids","volume":"52","author":"Scott","year":"1987","journal-title":"Vox Sang."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1046\/j.1365-2249.1998.00445.x","article-title":"Bacterial Lipopolysaccharide (LPS)-Specific Antibodies in Commercial Human Immunoglobulin Preparations: Superior Antibody Content of an IgM- Enriched Product","volume":"111","author":"Trautmann","year":"1998","journal-title":"Clin. Exp. Immunol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"453","DOI":"10.14573\/altex.1709221","article-title":"Material-Mediated Pyrogens in Medical Devices: Applicability of the in Vitro Monocyte Activation Test","volume":"207","author":"Borton","year":"2018","journal-title":"ALTEX"},{"key":"ref_164","first-page":"1","article-title":"Endotoxin Standards and CSE Potency","volume":"11","author":"Dawson","year":"1993","journal-title":"LAL Updat."},{"key":"ref_165","unstructured":"Chen, J., and Vinther, A. (2013). Low Endotoxin Recovery in Common Biologics Products, PDA Annual Meeting, PDA Annual Meeting."},{"key":"ref_166","first-page":"1","article-title":"Possible Mechanism of Low Endotoxin Recovery","volume":"17","author":"Tsuchiya","year":"2014","journal-title":"Am. Pharm. Rev."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"433","DOI":"10.5731\/pdajpst.2018.009464","article-title":"Sample Treatments That Solve Low Endotoxin Recovery Issues","volume":"73","author":"Tsuchiya","year":"2019","journal-title":"PDA J. Pharm. Sci. Technol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"462995","DOI":"10.1016\/j.chroma.2022.462995","article-title":"The Impact of Endotoxin Masking on the Removal of Endotoxin during Manufacturing of a Biopharmaceutical Drug Product","volume":"1671","author":"Wespel","year":"2022","journal-title":"J. Chromatogr. A"},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Correa, W., Brandenburg, K., Z\u00e4hringer, U., Ravuri, K., Khan, T., and Von Wintzingerode, F. (2017). Biophysical Analysis of Lipopolysaccharide Formulations for an Understanding of the Low Endotoxin Recovery (LER) Phenomenon. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18122737"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1038\/202811a0","article-title":"Restoration of Endotoxin Activity Following Alteration by Plasma","volume":"202","author":"Rudbach","year":"1964","journal-title":"Nature"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"41296","DOI":"10.1074\/jbc.M111.269225","article-title":"Structure and Function of Papiliocin with Antimicrobial and Anti-Inflammatory Activities Isolated from the Swallowtail Butterfly, Papilio xuthus","volume":"286","author":"Kim","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.peptides.2012.11.010","article-title":"Shrimp Anti-Lipopolysaccharide Factor (SALF), an Antimicrobial Peptide, Inhibits Proinflammatory Cytokine Expressions through the MAPK and NF-\u03baB Pathways in LPS-Induced HeLa Cells","volume":"40","author":"Lin","year":"2013","journal-title":"Peptides"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1159\/000315917","article-title":"Extracorporeal Removal of Endotoxin: The Polymyxin B-Immobilized Fiber Cartridge","volume":"Volume 167","author":"Tani","year":"2010","journal-title":"Contributions to Nephrology"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.ab.2014.08.018","article-title":"Detecting Endotoxin with a Flow Cytometry-Based Magnetic Aptasensor","volume":"466","author":"Zuo","year":"2014","journal-title":"Anal. Biochem."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"3410","DOI":"10.1021\/acsabm.1c00006","article-title":"Poly- l -Lysine-Functionalized Green-Light-Emitting Carbon Dots as a Fluorescence Turn-on Sensor for Ultrasensitive Detection of Endotoxin","volume":"4","author":"Thakur","year":"2021","journal-title":"ACS Appl. Bio Mater."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1016\/j.xphs.2015.10.028","article-title":"Quantitation of Polymyxin\u2013Lipopolysaccharide Interactions Using an Image-Based Fluorescent Probe","volume":"105","author":"McInerney","year":"2016","journal-title":"J. Pharm. Sci."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"671","DOI":"10.4014\/jmb.1801.01025","article-title":"Biophysical Studies Reveal Key Interactions between Papiliocin-Derived PapN and Lipopolysaccharide in Gram-Negative Bacteria","volume":"28","author":"Durai","year":"2018","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1046\/j.1432-1327.1998.2580686.x","article-title":"Biophysical Characterisation of Lysozyme Binding to LPS Re and Lipid A","volume":"258","author":"Brandenburg","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"e2115669119","DOI":"10.1073\/pnas.2115669119","article-title":"Molecular Mechanism Underlying the TLR4 Antagonistic and Antiseptic Activities of Papiliocin, an Insect Innate Immune Response Molecule","volume":"119","author":"Krishnan","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/s10989-012-9320-1","article-title":"A Novel Antimicrobial Peptide Derived from the Insect Paederus dermatitis","volume":"19","author":"Asoodeh","year":"2013","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"3282","DOI":"10.1016\/j.bbamem.2007.07.017","article-title":"Structural and Thermodynamic Analyses of the Interaction between Melittin and Lipopolysaccharide","volume":"1768","author":"Bhunia","year":"2007","journal-title":"BBA\u2014Biomembr."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1093\/infdis\/170.6.1490","article-title":"Synthetic Peptides That Mimic The Binding Site Of Horseshoe Crab Antilipopolysaccharide Factor","volume":"170","author":"Kloczewiak","year":"1994","journal-title":"J. Infect. Dis."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"19379","DOI":"10.1074\/jbc.M115.653196","article-title":"Factor B Is the Second Lipopolysaccharide-Binding Protease Zymogen in the Horseshoe Crab Coagulation Cascade","volume":"290","author":"Kobayashi","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1073\/pnas.0306904101","article-title":"A Serine Protease Zymogen Functions as a Pattern-Recognition Receptor for Lipopolysaccharides","volume":"101","author":"Ariki","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S1016-8478(23)10763-1","article-title":"Kinetics of Binding of LPS to Recombinant CD14, TLR4, and MD-2 Proteins","volume":"24","author":"Shin","year":"2007","journal-title":"Mol. Cells"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1042\/bj3120839","article-title":"Lactoferrin-Lipopolysaccharide Interaction: Involvement of the 28-34 Loop Region of Human Lactoferrin in the High-Affinity Binding to Escherichia Coli 055B5 Lipopolysaccharide","volume":"312","author":"Roseanu","year":"1995","journal-title":"Biochem. J."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1549931","DOI":"10.1080\/20002297.2018.1549931","article-title":"Aggregatibacter Actinomycetemcomitans LPS Binds Human Interleukin-8","volume":"11","author":"Ahlstrand","year":"2018","journal-title":"J. Oral Microbiol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"5067","DOI":"10.4049\/jimmunol.180.7.5067","article-title":"High Mobility Group Box 1 Protein Binding to Lipopolysaccharide Facilitates Transfer of Lipopolysaccharide to CD14 and Enhances Lipopolysaccharide-Mediated TNF-\u03b1 Production in Human Monocytes","volume":"180","author":"Youn","year":"2008","journal-title":"J. Immunol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/j.intimp.2004.02.004","article-title":"A Synthetic Peptide Derived from Bactericidal\/Permeability-Increasing Protein Neutralizes Endotoxin in Vitro and in Vivo","volume":"4","author":"Jiang","year":"2004","journal-title":"Int. Immunopharmacol."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"1672","DOI":"10.1128\/AAC.50.5.1672-1679.2006","article-title":"LL-37 Protects Rats against Lethal Sepsis Caused by Gram-Negative Bacteria","volume":"50","author":"Cirioni","year":"2006","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1021\/bc500094d","article-title":"Probing the Penetration of Antimicrobial Polymyxin Lipopeptides into Gram-Negative Bacteria","volume":"25","author":"Deris","year":"2014","journal-title":"Bioconjug. Chem."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"672589","DOI":"10.3389\/fmicb.2021.672589","article-title":"Lactosmart: A Novel Therapeutic Molecule for Antimicrobial Defense","volume":"12","author":"Singh","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Luo, J.-C., Zhang, J., and Sun, L. (2021). A G-Type Lysozyme from Deep-Sea Hydrothermal Vent Shrimp Kills Selectively Gram-Negative Bacteria. Molecules, 26.","DOI":"10.3390\/molecules26247624"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/S0014-5793(99)01600-2","article-title":"SMAP-29: A Potent Antibacterial and Antifungal Peptide from Sheep Leukocytes","volume":"463","author":"Skerlavaj","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"e02168-19","DOI":"10.1128\/AAC.02168-19","article-title":"Antibody Binding to the O-Specific Antigen of Pseudomonas Aeruginosa O6 Inhibits Cell Growth","volume":"64","author":"Richard","year":"2020","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.bcp.2005.04.040","article-title":"A Synthesized Cationic Tetradecapeptide from Hornet Venom Kills Bacteria and Neutralizes Lipopolysaccharide in Vivo and in Vitro","volume":"70","author":"Yibin","year":"2005","journal-title":"Biochem. Pharmacol."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"7263","DOI":"10.1002\/chem.202000495","article-title":"Increasing the Affinity of an O-Antigen Polysaccharide Binding Site in Shigella flexneri Bacteriophage Sf6 Tailspike Protein","volume":"26","author":"Kunstmann","year":"2020","journal-title":"Chem.\u2014A Eur. J."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"5144","DOI":"10.1021\/bi0020426","article-title":"Enthalpic Barriers to the Hydrophobic Binding of Oligosaccharides to Phage P22 Tailspike Protein","volume":"40","author":"Baxa","year":"2001","journal-title":"Biochemistry"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.1042\/BST0381386","article-title":"Carbohydrate Binding of Salmonella Phage P22 Tailspike Protein and Its Role during Host Cell Infection","volume":"38","author":"Andres","year":"2010","journal-title":"Biochem. Soc. Trans."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1093\/jmcb\/mjaa067","article-title":"SARS-CoV-2 Spike Protein Binds to Bacterial Lipopolysaccharide and Boosts Proinflammatory Activity","volume":"12","author":"Petruk","year":"2020","journal-title":"J. Mol. Cell Biol."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1096\/fj.99-0866com","article-title":"Definition of Endotoxin Binding Sites in Horseshoe Crab Factor C Recombinant Sushi Proteins and Neutralization of Endotoxin by Sushi Peptides","volume":"14","author":"Tan","year":"2000","journal-title":"FASEB J."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1099\/00221287-144-8-2179","article-title":"Attacin\u2014An Insect Immune Protein\u2014Binds LPS and Triggers the Specific Inhibition of Bacterial Outer-Membrane Protein Synthesis","volume":"144","author":"Carlsson","year":"1998","journal-title":"Microbiology"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"25987","DOI":"10.1074\/jbc.M114.586933","article-title":"The N-Terminal Arg Residue Is Essential for Autocatalytic Activation of a Lipopolysaccharide-Responsive Protease Zymogen","volume":"289","author":"Kobayashi","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/j.bbapap.2013.12.017","article-title":"Interaction between Tachyplesin I, an Antimicrobial Peptide Derived from Horseshoe Crab, and Lipopolysaccharide","volume":"1844","author":"Kushibiki","year":"2014","journal-title":"BBA\u2014Proteins Proteom."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"50150","DOI":"10.1074\/jbc.M405606200","article-title":"Perturbation of Lipopolysaccharide (LPS) Micelles by Sushi 3 (S3) Antimicrobial Peptide: The Importance of an Intermolecular Disulfide Bond in S3 Dimer for Binding, Disruption, and Neutralization of LPS","volume":"279","author":"Li","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/j.intimp.2008.01.015","article-title":"A Synthetic Cyclic Peptide Derived from Limulus Anti-Lipopolysaccharide Factor Neutralizes Endotoxin in Vitro and in Vivo","volume":"8","author":"Ren","year":"2008","journal-title":"Int. Immunopharmacol."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"e9","DOI":"10.1017\/S0033583517000075","article-title":"Lysozyme\u2019s Lectin-like Characteristics Facilitates Its Immune Defense Function","volume":"50","author":"Zhang","year":"2017","journal-title":"Q. Rev. Biophys."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"12270","DOI":"10.1074\/jbc.M112.411884","article-title":"The Novel Human \u03b2-Defensin 114 Regulates Lipopolysaccharide (LPS)-Mediated Inflammation and Protects Sperm from Motility Loss","volume":"288","author":"Yu","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"3395","DOI":"10.1007\/s00253-012-4588-9","article-title":"Human Beta-Defensin DEFB126 Is Capable of Inhibiting LPS-Mediated Inflammation","volume":"97","author":"Liu","year":"2013","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"10482","DOI":"10.1074\/jbc.270.18.10482","article-title":"Lipopolysaccharide Binding Protein-Mediated Complexation of Lipopolysaccharide with Soluble CD14","volume":"270","author":"Tobias","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"4754","DOI":"10.1128\/iai.60.11.4754-4761.1992","article-title":"High-Affinity Binding of the Bactericidal\/Permeability-Increasing Protein and a Recombinant Amino-Terminal Fragment to the Lipid A Region of Lipopolysaccharide","volume":"60","author":"Parent","year":"1992","journal-title":"Infect. Immun."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1111\/j.1574-6968.1991.tb04890.x","article-title":"Binding of a Histidine-Rich Peptide to Porphyromonas gingivalis","volume":"82","author":"Murakami","year":"1991","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"2628","DOI":"10.1128\/iai.62.6.2628-2632.1994","article-title":"Lactoferrin Is a Lipid A-Binding Protein","volume":"62","author":"Appelmelk","year":"1994","journal-title":"Infect. Immun."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1006\/bbrc.1998.9675","article-title":"Affinities of Different Proteins and Peptides for Lipopolysaccharide as Determined by Biosensor Technology","volume":"252","author":"Haas","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"3607","DOI":"10.4049\/jimmunol.161.7.3607","article-title":"A Synthetic Lipopolysaccharide-Binding Peptide Based on Amino Acids 27\u201339 of Serum Amyloid P Component Inhibits Lipopolysaccharide-Induced Responses in Human Blood","volume":"161","author":"Verhoef","year":"1998","journal-title":"J. Immunol."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"1291","DOI":"10.1128\/iai.63.4.1291-1297.1995","article-title":"Human CAP18: A Novel Antimicrobial Lipopolysaccharide-Binding Protein","volume":"63","author":"Larrick","year":"1995","journal-title":"Infect. Immun."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"2376","DOI":"10.1038\/s41598-020-59071-7","article-title":"Studies on Citrullinated LL-37: Detection in Human Airways, Antibacterial Effects and Biophysical Properties","volume":"10","author":"Wallin","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"2753","DOI":"10.1002\/eji.201141391","article-title":"Identification of Lipopolysaccharide-Binding Peptide Regions within HMGB1 and Their Effects on Subclinical Endotoxemia in a Mouse Model","volume":"41","author":"Youn","year":"2011","journal-title":"Eur. J. Immunol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1097\/01.shk.0000055236.26446.c9","article-title":"Neutralization of Endotoxin in Vitro and in Vivo by Bac7(1-35), a Proline-Rich Antibacterial Peptide","volume":"19","author":"Ghiselli","year":"2003","journal-title":"Shock"},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"694","DOI":"10.3390\/antibiotics3040694","article-title":"Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs","volume":"3","author":"Zughaier","year":"2014","journal-title":"Antibiotics"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"2581","DOI":"10.1111\/j.1742-4658.2006.05261.x","article-title":"Structure-Activity Relationships of Fowlicidin-1, a Cathelicidin Antimicrobial Peptide in Chicken","volume":"273","author":"Xiao","year":"2006","journal-title":"FEBS J."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/S0014-5793(99)00443-3","article-title":"Interactions of an Antimicrobial Peptide, Magainin 2, with Lipopolysaccharide-Containing Liposomes as a Model for Outer Membranes of Gram-Negative Bacteria","volume":"449","author":"Matsuzaki","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1007\/s00011-004-1300-2","article-title":"Antibacterial Cathelicidin Peptide CAP11 Inhibits the Lipopolysaccharide (LPS)-Induced Suppression of Neutrophil Apoptosis by Blocking the Binding of LPS to Target Cells","volume":"53","author":"Nagaoka","year":"2004","journal-title":"Inflamm. Res."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1186\/s13071-015-1176-8","article-title":"A Cecropin-like Antimicrobial Peptide with Anti-Inflammatory Activity from the Black Fly Salivary Glands","volume":"8","author":"Wu","year":"2015","journal-title":"Parasit. Vectors"},{"key":"ref_225","first-page":"1","article-title":"Aseptic Sampling Best Practices Endotoxin Binding Affinity","volume":"SP-4006-e","author":"Meadows","year":"2018","journal-title":"Sartorius"},{"key":"ref_226","first-page":"1","article-title":"The Problems with Plastics","volume":"6","author":"Novitsky","year":"1988","journal-title":"Lal Update"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1080\/01971520009349541","article-title":"Comparison of Blocking Agents for an ELISA for LPS","volume":"21","author":"Kocsis","year":"2000","journal-title":"J. Immunoass."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1016\/0011-2240(78)90081-0","article-title":"Nature of Freezing Damage on the Lipopolysaccharide Molecule of Escherichia coli B","volume":"15","author":"Kempler","year":"1978","journal-title":"Cryobiology"},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"1763","DOI":"10.1128\/aem.61.5.1763-1769.1995","article-title":"Influence of Various Dust Sampling and Extraction Methods on the Measurement of Airborne Endotoxin","volume":"61","author":"Douwes","year":"1995","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1128\/aem.42.5.843-849.1981","article-title":"Effect of Defined Lipopolysaccharide Core Defects on Resistance of Salmonella Typhimurium to Freezing and Thawing and Other Stresses","volume":"42","author":"Bennett","year":"1981","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1007\/s12275-019-9116-5","article-title":"Applications of Different Solvents and Conditions for Differential Extraction of Lipopolysaccharide in Gram-Negative Bacteria","volume":"57","author":"Nguyen","year":"2019","journal-title":"J. Microbiol."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/0003-2697(85)90442-7","article-title":"Measurement of Protein Using Bicinchoninic Acid","volume":"150","author":"Smith","year":"1985","journal-title":"Anal. Biochem."},{"key":"ref_233","doi-asserted-by":"crossref","unstructured":"Papadiamantis, A.G., Klaessig, F.C., Exner, T.E., Hofer, S., Hofstaetter, N., Himly, M., Williams, M.A., Doganis, P., Hoover, M.D., and Afantitis, A. (2020). Metadata Stewardship in Nanosafety Research: Community-Driven Organisation of Metadata Schemas to Support FAIR Nanoscience Data. Nanomaterials, 10.","DOI":"10.3390\/nano10102033"},{"key":"ref_234","unstructured":"(2023, February 12). PubMed Keyword \u201cEndotoxin\u201d 5203 Events, Keyword \u201cLipopolysaccharide\u201d 7853 Events, Available online: https:\/\/pubmed.ncbi.nlm.nih.gov\/."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/9\/8395\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T19:30:51Z","timestamp":1760124651000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/9\/8395"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,5,7]]},"references-count":234,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2023,5]]}},"alternative-id":["ijms24098395"],"URL":"https:\/\/doi.org\/10.3390\/ijms24098395","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,5,7]]}}}