{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T09:13:34Z","timestamp":1788858814484,"version":"build-2803163510"},"reference-count":153,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2023,11,7]],"date-time":"2023-11-07T00:00:00Z","timestamp":1699315200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>Sepsis is a life-threatening complication of an infectious process that results from the excessive and uncontrolled activation of the host\u2019s pro-inflammatory immune response to a pathogen. Lipopolysaccharide (LPS), also known as endotoxin, which is a major component of Gram-negative bacteria\u2019s outer membrane, plays a key role in the development of Gram-negative sepsis and septic shock in humans. To date, no specific and effective drug against sepsis has been developed. This review summarizes data on LPS-binding proteins from marine invertebrates (ILBPs) that inhibit LPS toxic effects and are of interest as potential drugs for sepsis treatment. The structure, physicochemical properties, antimicrobial, and LPS-binding\/neutralizing activity of these proteins and their synthetic analogs are considered in detail. Problems that arise during clinical trials of potential anti-endotoxic drugs are discussed.<\/jats:p>","DOI":"10.3390\/md21110581","type":"journal-article","created":{"date-parts":[[2023,11,7]],"date-time":"2023-11-07T00:44:18Z","timestamp":1699317858000},"page":"581","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Host Defense Proteins and Peptides with Lipopolysaccharide-Binding Activity from Marine Invertebrates and Their Therapeutic Potential in Gram-Negative Sepsis"],"prefix":"10.3390","volume":"21","author":[{"given":"Tamara Fedorovna","family":"Solov\u2019eva","sequence":"first","affiliation":[{"name":"G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Science, Vladivostok 690022, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Svetlana Ivanovna","family":"Bakholdina","sequence":"additional","affiliation":[{"name":"G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Science, Vladivostok 690022, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gennadii Alexandrovich","family":"Naberezhnykh","sequence":"additional","affiliation":[{"name":"G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Science, Vladivostok 690022, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,11,7]]},"reference":[{"key":"ref_1","first-page":"167","article-title":"Bacterial lipopolysaccharides and innate immunity","volume":"7","author":"Alexander","year":"2001","journal-title":"J. Endotoxin Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1086\/367990","article-title":"Blocking of responses to endotoxin by E5564 in healthy volunteers with experimental endotoxemia","volume":"187","author":"Lynn","year":"2003","journal-title":"J. Infect. Dis."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2216","DOI":"10.3390\/md11062216","article-title":"Marine compounds with therapeutic potential in Gram-negative sepsis","volume":"11","author":"Davydova","year":"2013","journal-title":"Mar. Drugs"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.2174\/1568026043388079","article-title":"Endotoxin neutralizing peptides","volume":"4","author":"Jerala","year":"2004","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_5","first-page":"128","article-title":"Recent advances in the innate immunity of invertebrate animals","volume":"38","author":"Iwanaga","year":"2005","journal-title":"J. Biochem. Mol. Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1034\/j.1600-065X.2000.917309.x","article-title":"Innate immune recognition: Mechanisms and pathways","volume":"173","author":"Medzhitov","year":"2000","journal-title":"Immunol. Rev."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/0006-291X(82)91493-0","article-title":"Limulus anti-LPS factor: An anticoagulant which inhibits the endotoxin-mediated activation of Limulus coagulation system","volume":"105","author":"Tanaka","year":"1982","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1093\/oxfordjournals.jbchem.a135218","article-title":"Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS)","volume":"97","author":"Morita","year":"1985","journal-title":"J. Biochem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1093\/oxfordjournals.jbchem.a121999","article-title":"Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus","volume":"101","author":"Muta","year":"1987","journal-title":"J. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1086\/514204","article-title":"Limulus anti-lipopolysaccharide factor prevents mortality late in the course of endotoxemia","volume":"177","author":"Roth","year":"1998","journal-title":"J. Infect. Dis."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2506","DOI":"10.1128\/iai.60.6.2506-2513.1992","article-title":"Binding and neutralization of endotoxin by limulus anti-lipopolysaccharide factor","volume":"60","author":"Warren","year":"1992","journal-title":"Infect. Immun."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1612","DOI":"10.1128\/iai.57.5.1612-1614.1989","article-title":"Anti-lipopolysaccharide factor from horseshoe crab, Tachypleus tridentatus, inhibits lipopolysaccharide activation of cultured human endothelial cells","volume":"57","author":"Desch","year":"1989","journal-title":"Infect. Immun."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1093\/infdis\/165.3.494","article-title":"Limulus antilipopolysaccharide factor protects rabbits from meningococcal endotoxin shock","volume":"165","author":"Alpert","year":"1992","journal-title":"J. Infect. Dis."},{"key":"ref_14","first-page":"104","article-title":"Efficacy of a recombinant endotoxin neutralizing protein in rabbits with Escherichia coli sepsis","volume":"42","author":"Saladino","year":"1994","journal-title":"Circ. Shock"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"123","DOI":"10.3354\/dao061123","article-title":"Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach","volume":"61","author":"Supungul","year":"2004","journal-title":"Dis. Aquat. Organ."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1007\/s10126-005-5006-4","article-title":"Molecular cloning and expression profile of putative antilipopolysaccharide factor in chinese shrimp (Fenneropenaeus chinensis)","volume":"7","author":"Liu","year":"2005","journal-title":"Mar. Biotechnol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1916","DOI":"10.1016\/j.molimm.2007.10.039","article-title":"Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): A broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection","volume":"45","author":"Shockey","year":"2008","journal-title":"Mol. Immunol."},{"key":"ref_18","first-page":"263","article-title":"Anti-lipopolysaccharide factors in the american lobster Homarus americanus: Molecular characterization and transcriptional response to Vibrio fluvialis challenge","volume":"3","author":"Beale","year":"2008","journal-title":"Comp. Biochem. Physiol. Part D Genom. Proteom."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1016\/j.dci.2010.04.002","article-title":"The second anti-lipopolysaccharide factor (EsALF-2) with antimicrobial activity from Eriocheir sinensis","volume":"34","author":"Zhang","year":"2010","journal-title":"Dev. Comp. Immunol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"3195","DOI":"10.1016\/j.molimm.2007.01.028","article-title":"Antilipopolysaccharide factor (ALF) of mud crab Scylla paramamosain: Molecular cloning, genomic organization and the antimicrobial activity of its synthetic LPS binding domain","volume":"44","author":"Imjongjirak","year":"2007","journal-title":"Mol. Immunol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.rinim.2011.06.001","article-title":"Molecular characterization and phylogenetic analysis of two antimicrobial peptides: Anti-lipopolysaccharide factor and crustin from the brown mud crab, Scylla serrata","volume":"1","author":"Afsal","year":"2011","journal-title":"Results Immunol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.aquaculture.2012.05.028","article-title":"A new isoform of anti-lipopolysaccharide factor identified from the blue swimmer crab, Portunus pelagicus: Molecular characteristics and phylogeny","volume":"356","author":"Afsal","year":"2012","journal-title":"Aquaculture"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1007\/s10126-011-9381-8","article-title":"Cationic antimicrobial peptides in Penaeid shrimp","volume":"13","author":"Tassanakajon","year":"2011","journal-title":"Mar. Biotechnol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/j.dci.2005.02.004","article-title":"Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon","volume":"29","author":"Somboonwiwat","year":"2005","journal-title":"Dev. Comp. Immunol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.fsi.2009.05.009","article-title":"Identification, cloning, characterization and recombinant expression of an anti-lipopolysaccharide factor from the hemocytes of indian mud crab, Scylla serrata","volume":"27","author":"Yedery","year":"2009","journal-title":"Fish Shellfish Immunol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.dci.2015.06.015","article-title":"Recombinant expression and functional analysis of an isoform of anti-lipopolysaccharide factors (FcALF5) from Chinese shrimp Fenneropenaeus chinensis","volume":"53","author":"Yang","year":"2015","journal-title":"Dev. Comp. Immunol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.fsi.2007.07.010","article-title":"Anti-lipopolysaccharide factors from the black tiger shrimp, Penaeus monodon, are encoded by two genomic loci","volume":"24","author":"Tharntada","year":"2008","journal-title":"Fish Shellfish Immunol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.fsi.2011.10.010","article-title":"Gene silencing reveals a crucial role for anti-lipopolysaccharide factors from Penaeus monodon in the protection against microbial infections","volume":"32","author":"Ponprateep","year":"2012","journal-title":"Fish Shellfish Immunol."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Li, S.H., Zhang, X.J., Sun, Z., Li, F.H., and Xiang, J.H. (2013). Transcriptome analysis on Chinese shrimp Fenneropenaeus chinensis during WSSV acute infection. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0058627"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.fsi.2011.02.016","article-title":"Multiple isoforms of immune-related genes from hemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus","volume":"31","author":"Liu","year":"2011","journal-title":"Fish Shellfish Immunol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/978-3-030-41769-7_3","article-title":"The anti-lipopolysaccharide factors in crustaceans","volume":"94","author":"Li","year":"2020","journal-title":"Subcell Biochem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2602","DOI":"10.3390\/md13052602","article-title":"Functional diversity of anti-lipopolysaccharide factor isoforms in shrimp and their characters related to antiviral activity","volume":"13","author":"Li","year":"2015","journal-title":"Mar. Drugs"},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Matos, G.M., Schmitt, P., Barreto, C., Farias, N.D., Toledo-Silva, G., Guzm\u00e1n, F., Destoumieux-Garz\u00f3n, D., Perazzolo, L.M., and Rosa, R.D. (2018). Massive gene expansion and sequence diversification is associated with diverse tissue distribution, regulation and antimicrobial properties of anti-lipopolysaccharide factors in shrimp. Mar. Drugs, 16.","DOI":"10.3390\/md16100381"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.fsi.2019.08.066","article-title":"Molecular and antimicrobial characterization of a group G anti-lipopolysaccharide factor (ALF) from Penaeus monodon","volume":"94","author":"Zhou","year":"2019","journal-title":"Fish Shellfish Immunol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.dci.2017.02.009","article-title":"A novel anti-lipopolysaccharide factor SpALF6 in mud crab Scylla paramamosain exhibiting different antimicrobial activity from its single amino acid mutant","volume":"72","author":"Hou","year":"2017","journal-title":"Dev. Comp. Immunol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3351","DOI":"10.1002\/j.1460-2075.1993.tb06008.x","article-title":"Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus antiLPS factor, at 1.5 A resolution","volume":"12","author":"Hoess","year":"1993","journal-title":"EMBO J."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1099\/vir.0.009621-0","article-title":"Role of antilipopolysaccharide factor from the black tiger shrimp, Penaeus monodon, in protection from white spot syndrome virus infection","volume":"90","author":"Tharntada","year":"2009","journal-title":"J. Gen. Virol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/j.intimp.2007.01.006","article-title":"Shrimp (Penaeus monodon) antilipopolysaccharide factor reduces the lethality of Pseudomonas aeruginosa sepsis in mice","volume":"7","author":"Pan","year":"2007","journal-title":"Int. Immunopharmacol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.dci.2014.03.003","article-title":"Modification of a synthetic LPS-binding domain of anti-lipopolysaccharide factor from shrimp reveals strong structure-activity relationship in their antimicrobial characteristics","volume":"45","author":"Guo","year":"2014","journal-title":"Dev. Comp. Immunol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1002\/bip.21119","article-title":"NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: Model of the possible lipid A-binding site","volume":"91","author":"Yang","year":"2009","journal-title":"Biopolymers"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1042\/BJ20070279","article-title":"Mechanism of interaction of optimized Limulus-derived cyclic peptides with endotoxins: Thermodynamic, biophysical and microbiological analysis","volume":"406","author":"Howe","year":"2007","journal-title":"Biochem. J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"3817","DOI":"10.1128\/AAC.00534-10","article-title":"New antiseptic peptides to protect against endotoxin mediated shock","volume":"54","author":"Gutsmann","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.febslet.2004.10.012","article-title":"Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina","volume":"577","author":"Ovchinnikova","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_44","unstructured":"Nielsen, A.K., Sandvang, D., Neve, S., Kruse, T., and Kristensen, H.H. (2010, January 12\u201315). Transcriptional profiling indicates a dual mode-of-action of arenicin-3, poster F1-2072. Proceedings of the 50th Interscience Conference on Antimicrobial Agents and Chemotherapy, Boston, MA, USA."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.bbrc.2007.06.029","article-title":"Recombinant expression, synthesis, purification, and solution structure of arenicin","volume":"360","author":"Ovchinnikova","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3184","DOI":"10.1038\/s41467-020-16950-x","article-title":"An amphipathic peptide with antibiotic activity against multidrug-resistant Gram-negative bacteria","volume":"11","author":"Elliott","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"6255","DOI":"10.1021\/bi200746t","article-title":"Molecular mechanism of action of \u03b2-hairpin antimicrobial peptide arenicin: Oligomeric structure in dodecylphosphocholine micelles and pore formation in planar lipid bilayers","volume":"50","author":"Shenkarev","year":"2011","journal-title":"Biochemistry"},{"key":"ref_48","first-page":"455","article-title":"Molecular insight into mechanism of antimicrobial action of the \u03b2-hairpin peptide arenicin: Specific oligomerization in detergent micelles","volume":"89","author":"Ovchinnikova","year":"2008","journal-title":"Biopolym. Orig. Res. Biomol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1042\/BJ20071051","article-title":"Structure and mode of action of the antimicrobial peptide arenicin","volume":"410","author":"Jakovkin","year":"2008","journal-title":"Biochem. J."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"3392","DOI":"10.1038\/s41598-017-03664-2","article-title":"Antibacterial and detoxifying activity of NZ17074 analogues with multi-layers of selective antimicrobial actions against Escherichia coli and Salmonella enteritidis","volume":"7","author":"Yang","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e01056-16","DOI":"10.1128\/AAC.01056-16","article-title":"Combined systems approaches reveal a multistage mode of action of a marine antimicrobial peptide against pathogenic Escherichia coli and its protective effect against bacterial peritonitis and endotoxemia","volume":"61","author":"Wang","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_52","unstructured":"Hoegenhaug, H.H.K., Mygind, P.H., Kruse, T., Segura, D.R., Sandvang, D., and Neve, S. (2011). Antimicrobial Peptide Variants and Polynucleotides Encoding Same. (20110306750 A1), US Patent."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1093\/oxfordjournals.jbchem.a122913","article-title":"Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II. Chemical structures and biological activity","volume":"106","author":"Miyata","year":"1989","journal-title":"J. Biochem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"16709","DOI":"10.1016\/S0021-9258(18)37448-9","article-title":"Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus): Isolation and chemical structure","volume":"263","author":"Nakamura","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1093\/oxfordjournals.jbchem.a123191","article-title":"Tachyplesins isolated from hemocytes of southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): Identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor","volume":"108","author":"Muta","year":"1990","journal-title":"J. Biochem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"S0021","DOI":"10.1016\/S0021-9258(17)45367-1","article-title":"Antimicrobial tachyplesin peptide precursor cDNA cloning and cellular localization in the horseshoe crab (Tachypleus tridentatus)","volume":"265","author":"Shigenaga","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"15365","DOI":"10.1016\/S0021-9258(18)55402-8","article-title":"Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). NMR determination of the beta-sheet structure","volume":"265","author":"Kawano","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"12359","DOI":"10.1021\/bi026185z","article-title":"Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives","volume":"41","author":"Laederach","year":"2002","journal-title":"Biochemistry"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.bbapap.2003.12.009","article-title":"Structure-activity relationships for the \u03b2-hairpin cationic antimicrobial peptide polyphemusin I","volume":"1698","author":"Powers","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Vernen, F., Harvey, P.J., Dias, S.A., Veiga, A.S., Huang, Y.-H., Craik, D.J., Lawrence, N., and Troeira Henriques, S. (2019). Characterization of tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20174184"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/S0005-2736(02)00358-9","article-title":"Specific interactions of the antimicrobial peptide cyclic \u03b2-sheet tachyplesin I with lipopolysaccharides","volume":"1562","author":"Hirakura","year":"2002","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_62","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":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"14504","DOI":"10.1021\/bi0011173","article-title":"Interaction of polyphemusin I and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers","volume":"39","author":"Zhang","year":"2000","journal-title":"Biochemistry"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1021\/acsinfecdis.6b00045","article-title":"Contribution of amphipathicity and hydrophobicity to the antimicrobial activity and cytotoxicity of \u03b2-hairpin peptides","volume":"2","author":"Edwards","year":"2016","journal-title":"ACS Infect. Dis."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"6067","DOI":"10.1128\/AAC.00640-16","article-title":"Experimental induction of bacterial resistance to the antimicrobial peptide tachyplesin I and investigation of the resistance mechanisms","volume":"60","author":"Hong","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1096\/fj.09-143388","article-title":"Antimicrobial peptides from marine invertebrates as a new frontier for microbial infection control","volume":"24","author":"Magalhaes","year":"2010","journal-title":"FASEB J."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"15504","DOI":"10.1021\/bi051302m","article-title":"Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes","volume":"44","author":"Powers","year":"2005","journal-title":"Biochemistry"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1093\/oxfordjournals.jbchem.a124818","article-title":"Novel big defensin identified in horseshoe crab hemocytes: Isolation, amino acid sequence, and antibacterial activity","volume":"117","author":"Saito","year":"1995","journal-title":"J. Biochem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"10611","DOI":"10.1021\/bi800957n","article-title":"A Novel beta-defensin structure: A potential strategy of big defensin for overcoming resistance by Gram-positive bacteria","volume":"47","author":"Kouno","year":"2008","journal-title":"Biochemistry"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"7629","DOI":"10.1021\/bi900756y","article-title":"novel beta-defensin structure: Big defensin changes its N-terminal structure to associate with the target membrane","volume":"48","author":"Kouno","year":"2009","journal-title":"Biochemistry"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1016\/j.bbamem.2006.07.007","article-title":"The human beta-defensin-3, an antibacterial peptide with multiple biological functions","volume":"1758","author":"Dhople","year":"2006","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Perrigault, M., Tanguy, A., and Allam, B. (2009). Identification and expression of differentially expressed genes in the hard clam, Mercenaria mercenaria, in response to quahog parasite unknown (QPX). BMC Genom., 10.","DOI":"10.1186\/1471-2164-10-377"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Rosa, R.D., Santini, A., Fievet, J., Bulet, P., Destoumieux-Garz\u00f3n, D., and Bach\u00e8re, E. (2011). Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025594"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.fsi.2016.07.030","article-title":"Cloning of a big defensin gene and its response to Vibrio parahaemolyticus challenge in the noble scallop Chlamys nobilis (Bivalve: Pectinidae)","volume":"56","author":"Yang","year":"2016","journal-title":"Fish Shellfish Immunol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.fsi.2012.01.007","article-title":"The first chordate big defensin: Identification, expression and bioactivity","volume":"32","author":"Teng","year":"2012","journal-title":"Fish Shellfish Immunol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"e01821-19","DOI":"10.1128\/mBio.01821-19","article-title":"The ancestral N-terminal domain of big defensins drives bacterially triggered assembly into antimicrobial nanonets","volume":"10","author":"Loth","year":"2019","journal-title":"mBio"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.molimm.2006.02.025","article-title":"Molecular cloning, expression of a big defensin gene from bay scallop Argopecten irradians and the antimicrobial activity of its recombinant protein","volume":"44","author":"Zhao","year":"2007","journal-title":"Mol. Immunol."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Zhao, J., Li, C., Chen, A., Li, L., Su, X., and Li, T. (2010). Molecular characterization of a novel big defensin from clam Venerupis philippinarum. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0013480"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S0167-7799(01)01694-8","article-title":"A new era in pyrogen testing","volume":"19","author":"Ding","year":"2001","journal-title":"Trends Biotechnol."},{"key":"ref_80","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_81","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_82","doi-asserted-by":"crossref","unstructured":"Piehler, M., Roeder, R., Blessing, S., and Reich, J. (2020). Comparison of LAL and rFC assays-participation in a proficiency test program between 2014 and 2019. Microorganisms, 8.","DOI":"10.3390\/microorganisms8030418"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1177\/0968051907079573","article-title":"Recombinant factor C competes against LBP to bind lipopolysaccharide and neutralizes the endotoxicity","volume":"13","author":"Li","year":"2007","journal-title":"J. Endotoxin Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1111\/j.1432-1033.1986.tb09427.x","article-title":"Lipopolysaccharide-sensitive serine-protease zymogen (factor C) found in Limulus hemocytes: Isolation and characterization","volume":"154","author":"Nakamura","year":"1986","journal-title":"Eur. J. Biochem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1111\/j.1432-1033.1987.tb13352.x","article-title":"Lipopolysaccharide-sensitive serine-protease zymogen (factor C) of horseshoe crab hemocytes. Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease","volume":"167","author":"Tokunaga","year":"1987","journal-title":"Eur. J. Biochem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1093\/oxfordjournals.jbchem.a123337","article-title":"Further studies on lipopolysaccharide-sensitive serine protease zymogen (factor C): Its isolation from Limulus polyphemus hemocytes and identification as an intracellular zymogen activated by \u03b1-chymotrypsin, not by trypsin","volume":"109","author":"Tokunaga","year":"1991","journal-title":"J. Biochem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/0167-4838(93)90076-4","article-title":"Two forms of factor C from the amoebocytes of Carcinoscorpius rotundicauda: Purification and characterization","volume":"1202","author":"Ding","year":"1993","journal-title":"Biochim. Biophys. Acta Protein Struct. Mol. Enzymol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"6554","DOI":"10.1016\/S0021-9258(18)38153-5","article-title":"Limulus factor C. An endotoxin-sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains","volume":"266","author":"Muta","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"5751","DOI":"10.1046\/j.1432-1327.2000.01641.x","article-title":"The LCCL module","volume":"267","author":"Trexler","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/0022-2836(91)90666-T","article-title":"Three-dimensional structure of a complement control protein module in solution","volume":"219","author":"Norman","year":"1991","journal-title":"J. Mol. Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"7669","DOI":"10.1016\/S0021-9258(19)43242-0","article-title":"Epidermal growth factor. Location of disulfide bonds","volume":"248","author":"Savage","year":"1973","journal-title":"J. Biol. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"5974","DOI":"10.1021\/bi00141a004","article-title":"Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding","volume":"31","author":"Ullner","year":"1992","journal-title":"Biochemistry"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"34913","DOI":"10.1074\/jbc.M102874200","article-title":"Crystal structure of human epidermal growth factor and its dimerization","volume":"276","author":"Lu","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1111\/j.1432-1033.1988.tb14254.x","article-title":"Intracellular serine protease zymogen factor C, from horseshoe crab hemocytes: Its activation by synthetic lipid A analogues and acidic phospholipids","volume":"176","author":"Nakamura","year":"1988","journal-title":"Eur. J. Biochem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1093\/oxfordjournals.jbchem.a122276","article-title":"Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes","volume":"103","author":"Nakamura","year":"1988","journal-title":"J. Biochem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1096\/fasebj.14.7.859","article-title":"High-affinity LPS binding domain(s) in recombinant factor C of a horseshoe crab neutralizes LPS-induced lethality","volume":"14","author":"Tan","year":"2000","journal-title":"FASEB J."},{"key":"ref_97","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_98","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.1021\/jm049217k","article-title":"Structure of a synthetic fragment of the LALF protein when bound to lipopolysaccharide","volume":"48","author":"Pristovsek","year":"2005","journal-title":"J. Med. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"36363","DOI":"10.1074\/jbc.M202837200","article-title":"Modular arrangement and secretion of a multidomain serine protease. Evidence for involvement of proline-rich region and N-glycans in the secretion pathway","volume":"277","author":"Wang","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"13479","DOI":"10.1016\/S0021-9258(18)68262-6","article-title":"A family of lipopolysaccharide binding proteins involved in responses to Gram-negative sepsis","volume":"263","author":"Tobias","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1189\/jlb.0604320","article-title":"Antimicrobial proteins and peptides: Anti-infective molecules of mammalian leukocytes","volume":"76","author":"Levy","year":"2004","journal-title":"J. Leukoc. Biol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"10973","DOI":"10.1073\/pnas.94.20.10973","article-title":"An opsonic function of the neutrophil bactericidal\/permeability-increasing protein depends on both its N- and C-terminal domains","volume":"94","author":"Iovine","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1042\/bst0310785","article-title":"Bactericidal\/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): Structure, function and regulation in host defence against Gram-negative bacteria","volume":"31","author":"Weiss","year":"2003","journal-title":"Biochem. Soc. Trans."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"100105","DOI":"10.1016\/j.jtauto.2021.100105","article-title":"Killing three birds with one BPI: Bactericidal, opsonic, and anti-inflammatory functions","volume":"4","author":"Theprungsirikul","year":"2021","journal-title":"J. Transl. Autoimmun."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1172\/JCI107915","article-title":"Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli","volume":"55","author":"Weiss","year":"1975","journal-title":"J. Clin. Investig."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"2664","DOI":"10.1016\/S0021-9258(17)40872-6","article-title":"Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes","volume":"253","author":"Weiss","year":"1978","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1126\/science.276.5320.1861","article-title":"Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution","volume":"276","author":"Beamer","year":"1997","journal-title":"Science"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1006\/jmbi.2000.3805","article-title":"The 1.7 A crystal structure of BPI: A study of how two dissimilar amino acid sequences can adopt the same fold","volume":"299","author":"Kleiger","year":"2000","journal-title":"J. Mol. Biol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1042\/BST0391039","article-title":"LBP\/BPI proteins and their relatives: Conservation over evolution and roles in mutualism","volume":"39","author":"Krasity","year":"2011","journal-title":"Biochem. Soc. Trans."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"17759","DOI":"10.1073\/pnas.0702281104","article-title":"Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI","volume":"104","author":"Gonzalez","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1016\/S0021-9258(17)42107-7","article-title":"Functional domains of recombinant bactericidal\/permeability increasing protein (rBPI23)","volume":"269","author":"Little","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"4789","DOI":"10.4049\/jimmunol.156.12.4789","article-title":"Both N- and C-terminal regions of the bioactive N-terminal fragment of the neutrophil granule bactericidal\/permeability-increasing protein are required for stability and function","volume":"156","author":"Capodici","year":"1996","journal-title":"J. Immunol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"906","DOI":"10.1002\/pro.5560070408","article-title":"The BPI\/LBP family of proteins: A structural analysis of conserved regions","volume":"7","author":"Beamer","year":"1998","journal-title":"Protein Sci."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1006\/prep.1996.0071","article-title":"Expression and characterization of cysteine-modified variants of an amino-terminal fragment of bactericidal\/permeability-increasing protein","volume":"8","author":"Horwitz","year":"1996","journal-title":"Protein Expr. Purif."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1172\/JCI109707","article-title":"Resistance of Gram-negative bacteria to purified bactericidal leukocyte proteins: Relation to binding and bacterial lipopolysaccharide structure","volume":"65","author":"Weiss","year":"1980","journal-title":"J. Clin. Investig."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1128\/iai.62.1.259-265.1994","article-title":"Effect of lipopolysaccharide (LPS) chain length on interactions of bactericidal\/permeability-increasing protein and its bioactive 23-kilodalton NH2-terminal fragment with isolated LPS and intact Proteus mirabilis and Escherichia coli","volume":"62","author":"Capodici","year":"1994","journal-title":"Infect. Immun."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1016\/j.fsi.2011.01.031","article-title":"The second bactericidal permeability increasing protein (BPI) and its revelation of the gene duplication in the Pacific oyster, Crassostrea gigas","volume":"30","author":"Zhang","year":"2011","journal-title":"Fish Shellfish Immunol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"e00040-17","DOI":"10.1128\/mBio.00040-17","article-title":"Bactericidal permeability-increasing proteins shape host-microbe interactions","volume":"8","author":"Chen","year":"2017","journal-title":"mBio"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1186\/1742-9994-4-18","article-title":"Analysis of the immune-related transcriptome of a lophotrochozoan model, the marine annelid, Platynereis dumerilii","volume":"4","author":"Altincicek","year":"2007","journal-title":"Front. Zool."},{"key":"ref_120","first-page":"309","article-title":"Immune response of the Antarctic Sea urchin Sterechinus neumayeri: Cellular, molecular and physiological approach","volume":"63","author":"Urtubia","year":"2015","journal-title":"Rev. Biol. Trop."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1016\/j.fsi.2013.05.025","article-title":"Identification and expression analysis on bactericidal permeability-increasing protein (BPI)\/lipopolysaccharide-binding protein (LBP) of ark shell, Scapharca broughtonii","volume":"35","author":"Mao","year":"2013","journal-title":"Fish Shellfish Immunol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"34844","DOI":"10.1074\/jbc.M112.399998","article-title":"The bactericidal activity of the C-type lectin RegIII\u03b2 against Gram-negative bacteria involves binding to lipid A","volume":"287","author":"Miki","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1042\/BJ20051108","article-title":"Ligand specificities and structural requirements of two Tachypleus plasma lectins for bacterial trapping","volume":"393","author":"Kuo","year":"2006","journal-title":"Biochem. J."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"14493","DOI":"10.1074\/jbc.270.24.14493","article-title":"A novel type of Limulus lectin-L6\u2014Purification, primary structure, and antibacterial activity","volume":"270","author":"Saito","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"31008","DOI":"10.1074\/jbc.270.52.31008","article-title":"Purification, characterization, and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes","volume":"270","author":"Okino","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0145-305X(99)00019-1","article-title":"Role of lectins in the innate immunity of horseshoe crab","volume":"23","author":"Kawabata","year":"1999","journal-title":"Dev. Comp. Immunol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"3272","DOI":"10.1074\/jbc.274.6.3272","article-title":"A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides","volume":"274","author":"Inamori","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"30703","DOI":"10.1074\/jbc.272.49.30703","article-title":"A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides","volume":"272","author":"Saito","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"9631","DOI":"10.1074\/jbc.M008414200","article-title":"Biochemical properties and cDNa cloning of two new lectins from the plasma of Tachypleus tridentatus: Tachypleus plasma lectin 1 and 2","volume":"276","author":"Chen","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Ng, S.K., Huang, Y.T., Lee, Y.C., Low, E.L., Chiu, C.H., Chen, S.L., Mao, L.C., and Chang, M.D.T. (2014). A recombinant horseshoe crab plasma lectin recognizes specific pathogen-associated molecular patterns of bacteria through rhamnose. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0115296"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1630","DOI":"10.1074\/jbc.275.3.1630","article-title":"Isolation and characterization of proteins that bind to galactose, lipopolysaccharide of Escherichia coli, and protein A of Staphylococcus aureus from the hemolymph of Tachypleus tridentatus","volume":"275","author":"Chiou","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"2313","DOI":"10.1093\/emboj\/18.9.2313","article-title":"Tachylectin-2: Crystal structure of a specific GlcNAc\/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus","volume":"18","author":"Beisel","year":"1999","journal-title":"EMBO J."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1177\/09680519020080061201","article-title":"Molecular basis of non-self recognition by the horseshoe crab lectins","volume":"8","author":"Kawabata","year":"2002","journal-title":"J. Endotoxin Res."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"32810","DOI":"10.1074\/jbc.M304116200","article-title":"Emergence and disappearance of an immune molecule, an antimicrobial lectin, in basal metazoa: A tachylectin-related protein in the sponge Suberites domuncula","volume":"278","author":"Schroder","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1074\/jbc.275.2.1337","article-title":"Lipopolysaccharide- and b-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus: Purification, characterization, and cDNA cloning","volume":"275","author":"Lee","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.dci.2016.07.006","article-title":"Lipopolysaccharide- and \u03b2-1,3-glucan-binding protein from Fenneropenaeus merguiensis functions as a pattern recognition receptor with a broad specificity for diverse pathogens in the defense against microorganisms","volume":"67","author":"Chaosomboon","year":"2017","journal-title":"Dev. Comp. Immunol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.dci.2016.03.017","article-title":"Lipopolysaccharide and beta-1, 3-glucan binding protein (LGBP) stimulates prophenoloxidase activating system in Chinese mitten crab (Eriocheir sinensis)","volume":"61","author":"Zhang","year":"2016","journal-title":"Dev. Comp. Immunol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1016\/j.fsi.2012.01.020","article-title":"A scallop C-type lectin from Argopecten irradians (AiCTL5) with activities of lipopolysaccharide binding and Gram-negative bacteria agglutination","volume":"32","author":"Mu","year":"2012","journal-title":"Fish Shellfish Immunol."},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Amparyup, P., Sutthangkul, J., Charoensapsri, W., and Tassanakajon, A. (2016). Pattern recognition protein binds to lipopolysaccharide and \u03b2-1,3-glucan and activates shrimp prophenoloxidase system. J. Biol. Chem., 291.","DOI":"10.1074\/jbc.A111.294744"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/j.fsi.2010.07.025","article-title":"CfLGBP, a pattern recognition receptor in Chlamys farreri involved in the immune response against various bacteria","volume":"29","author":"Yang","year":"2010","journal-title":"Fish Shellfish Immunol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1134\/S1063074014010027","article-title":"Invertebrates of the Sea of Okhotsk as new sources of lipopolysaccharide binding proteins","volume":"40","author":"Bakholdina","year":"2014","journal-title":"Russ. J. Mar. Biol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.3390\/md12031471","article-title":"The role of biophysical parameters in the antilipopolysaccharide activities of antimicrobial peptides from marine fish","volume":"12","author":"Gopal","year":"2014","journal-title":"Mar. Drugs"},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Rosa, R.D., Vergnes, A., de Lorgeril, J., Goncalves, P., Perazzolo, L.M., Saun\u00e9, L., Romestand, B., Fievet, J., Gueguen, Y., and Bach\u00e8re, E. (2013). Functional divergence in shrimp anti-lipopolysaccharide factors (ALFs): From recognition of cell wall components to antimicrobial activity. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0067937"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1613","DOI":"10.1016\/j.bbamem.2012.03.015","article-title":"Structure, activity and interactions of the cysteine deleted analog of tachyplesin-1 with lipopolysaccharide micelle: Mechanistic insights into outer-membrane permeabilization and endotoxin neutralization","volume":"1818","author":"Saravanan","year":"2012","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"3883","DOI":"10.1074\/jbc.M109.065672","article-title":"NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: Mechanism of outer membrane permeabilization","volume":"285","author":"Bhunia","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1021\/bi900724x","article-title":"Effect of the hydrophobicity to net positive charge ratio on antibacterial and anti-endotoxin activities of structurally similar antimicrobial peptides","volume":"49","author":"Rosenfeld","year":"2010","journal-title":"Biochemistry"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"167572","DOI":"10.1155\/2015\/167572","article-title":"Inhibitory effects of antimicrobial peptides on lipopolysaccharide-induced inflammation","volume":"2015","author":"Sun","year":"2015","journal-title":"Mediat. Inflamm."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"18417","DOI":"10.1021\/ja1083255","article-title":"Structure, interactions, and antibacterial activities of MSI-594 derived mutant peptide MSI-594F5A in lipopolysaccharide micelles: Role of the helical hairpin conformation in outer-membrane permeabilization","volume":"132","author":"Domadia","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Ron\u010devi\u0107, T., Puizina, J., and Tossi, A. (2019). Antimicrobial peptides as anti-infective agents in pre-post-antibiotic era?. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20225713"},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Maximiano, M.R., Rios, T.B., Campos, M.L., Prado, G.S., Dias, S.C., and Franco, O.L. (2022). Nanoparticles in association with antimicrobial peptides (NanoAMPs) as a promising combination for agriculture development. Front. Mol. Biosci., 9.","DOI":"10.3389\/fmolb.2022.890654"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.ejmech.2015.03.028","article-title":"PEGylation of the peptide Bac7 (1-35) reduces renal clearance while retaining antibacterial activity and bacterial cell penetration capacity","volume":"95","author":"Benincasa","year":"2015","journal-title":"Eur. J. Med. Chem."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1134\/S0026893319050108","article-title":"Mouse Models of Sepsis and Septic Shock","volume":"53","author":"Korneev","year":"2019","journal-title":"Mol. Biol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.it.2014.07.004","article-title":"Host defense peptides: Front-line immunomodulators","volume":"35","author":"Mansour","year":"2014","journal-title":"Trends Immunol."}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/21\/11\/581\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T21:18:30Z","timestamp":1760131110000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/21\/11\/581"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,11,7]]},"references-count":153,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2023,11]]}},"alternative-id":["md21110581"],"URL":"https:\/\/doi.org\/10.3390\/md21110581","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,11,7]]}}}