{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T19:57:03Z","timestamp":1778788623225,"version":"3.51.4"},"reference-count":80,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2019,1,18]],"date-time":"2019-01-18T00:00:00Z","timestamp":1547769600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The endoplasmic reticulum (ER) chaperone protein, calreticulin (CRT), is essential for proper glycoprotein folding and maintaining cellular calcium homeostasis. During ER stress, CRT is overexpressed as part of the unfolded protein response (UPR). In addition, CRT can be released as a damage-associated molecular pattern (DAMP) molecule that may interact with pathogen-associated molecular patterns (PAMPs) during the innate immune response. One such PAMP is lipopolysaccharide (LPS), a component of the gram-negative bacterial cell wall. In this report, we show that recombinant and native human placental CRT strongly interacts with LPS in solution, solid phase, and the surface of gram-negative and gram-positive bacteria. Furthermore, LPS induces oilgomerization of CRT with a disappearance of the monomeric form. The application of recombinant CRT (rCRT) to size exclusion and anion exchange chromatography shows an atypical heterogeneous elution profile, indicating that LPS affects the conformation and ionic charge of CRT. Interestingly, LPS bound to CRT is detected in sera of bronchiectasis patients with chronic bacterial infections. By ELISA, rCRT dose-dependently bound to solid phase LPS via the N- and C-domain globular head region of CRT and the C-domain alone. The specific interaction of CRT with LPS may be important in PAMP innate immunity.<\/jats:p>","DOI":"10.3390\/ijms20020408","type":"journal-article","created":{"date-parts":[[2019,1,18]],"date-time":"2019-01-18T11:26:55Z","timestamp":1547810815000},"page":"408","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["The Biophysical Interaction of the Danger-Associated Molecular Pattern (DAMP) Calreticulin with the Pattern-Associated Molecular Pattern (PAMP) Lipopolysaccharide"],"prefix":"10.3390","volume":"20","author":[{"given":"Unnati M.","family":"Pandya","sequence":"first","affiliation":[{"name":"New York University School of Medicine--Langone Health, Departments of Medicine and Pathology, Division of Translational Medicine, 550 First Ave, New York, NY 10016, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chinaza","family":"Egbuta","sequence":"additional","affiliation":[{"name":"New York University School of Medicine--Langone Health, Departments of Medicine and Pathology, Division of Translational Medicine, 550 First Ave, New York, NY 10016, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Trefa M.","family":"Abdullah Norman","sequence":"additional","affiliation":[{"name":"University of Exeter Medical School, Exeter EX1 2LU, Devon UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chih-Yuan (Edward)","family":"Chiang","sequence":"additional","affiliation":[{"name":"Target Discovery and Experimental Microbiology Department, Molecular and Translational Sciences Division, US Army Research Institute of Infectious Diseases, Frederick, MD 21702, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Valerie R.","family":"Wiersma","sequence":"additional","affiliation":[{"name":"Department of Hematology, University Medical Center Groningen, University of Groningen, 9713GZ Groningen, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rekha G.","family":"Panchal","sequence":"additional","affiliation":[{"name":"Target Discovery and Experimental Microbiology Department, Molecular and Translational Sciences Division, US Army Research Institute of Infectious Diseases, Frederick, MD 21702, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Edwin","family":"Bremer","sequence":"additional","affiliation":[{"name":"Department of Hematology, University Medical Center Groningen, University of Groningen, 9713GZ Groningen, The Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul","family":"Eggleton","sequence":"additional","affiliation":[{"name":"University of Exeter Medical School, Exeter EX1 2LU, Devon UK"},{"name":"UCB Pharma, Slough SL1 3WE, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Leslie I","family":"Gold","sequence":"additional","affiliation":[{"name":"New York University School of Medicine--Langone Health, Departments of Medicine and Pathology, Division of Translational Medicine, 550 First Ave, New York, NY 10016, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2019,1,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/S0143416002001884","article-title":"Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum","volume":"32","author":"Michalak","year":"2002","journal-title":"Cell Calcium"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1007\/s12192-015-0638-4","article-title":"Unfolding the complexities of ER chaperones in health and disease: Report on the 11th international calreticulin workshop","volume":"20","author":"Gold","year":"2015","journal-title":"Cell Stress Chaperones"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1042\/BJ20081847","article-title":"Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum","volume":"417","author":"Michalak","year":"2009","journal-title":"Biochem. 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