{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T16:18:04Z","timestamp":1790007484615,"version":"4.0.1"},"reference-count":35,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2000,3,1]],"date-time":"2000-03-01T00:00:00Z","timestamp":951868800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2000,3,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>CD14 participates in the host innate inflammatory response to bacterial LPS obtained from Escherichia coli and other Gram-negative bacteria. Evidence from several laboratories suggests that different regions of the amino-terminal portion of the molecule may be involved in LPS binding. In this report a series of single-residue serine replacement and charge reversal mutations were generated to further elucidate the mechanism by which this protein may bind a multitude of different LPS ligands. Single-residue CD14 mutation proteins were examined for their ability to bind LPS obtained from E. coli, Porphyromonas gingivalis, and Helicobacter pylori and facilitate the activation of E-selectin from human endothelial cells. In addition, the single-residue CD14 mutation proteins were employed to perform monoclonal epitope-mapping studies with three LPS-blocking Abs that bound tertiary epitopes. Evidence that several different hydrophilic regions of the amino-terminal region of CD14 are involved in LPS binding was obtained. Epitope-mapping studies revealed that these hydrophilic regions are located on one side of the protein surface. These studies suggest that CD14 employs a charged surface in a manor similar to the macrophage scavenger receptor to \u201ccapture\u201d LPS ligands and \u201cpresent\u201d them to other components of the innate host defense system.<\/jats:p>","DOI":"10.4049\/jimmunol.164.6.3255","type":"journal-article","created":{"date-parts":[[2014,4,22]],"date-time":"2014-04-22T16:28:33Z","timestamp":1398184113000},"page":"3255-3263","source":"Crossref","is-referenced-by-count":63,"title":["CD14 Employs Hydrophilic Regions to \u201cCapture\u201d Lipopolysaccharides"],"prefix":"10.1093","volume":"164","author":[{"given":"Mark D","family":"Cunningham","sequence":"first","affiliation":[{"name":"Bristol-Myers Squibb Pharmaceutical Research Institute , Lawrenceville, NJ 08543"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert A","family":"Shapiro","sequence":"additional","affiliation":[{"name":"Department of Psychiatry and Behavioral Sciences, University of Washington , Seattle, WA 98195"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carrie","family":"Seachord","sequence":"additional","affiliation":[{"name":"Bristol-Myers Squibb Pharmaceutical Research Institute , Lawrenceville, NJ 08543"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kent","family":"Ratcliffe","sequence":"additional","affiliation":[{"name":"Immunex Corp. , Seattle, WA 98101"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Linda","family":"Cassiano","sequence":"additional","affiliation":[{"name":"Immunex Corp. , Seattle, WA 98101"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard P","family":"Darveau","sequence":"additional","affiliation":[{"name":"Department of Periodontics, University of Washington , Seattle, WA 98195"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2000,3,15]]},"reference":[{"key":"2026020213173600000_R1","first-page":"1431","volume-title":"Science","year":"1990"},{"key":"2026020213173600000_R2","first-page":"1429","volume-title":"Science","year":"1990"},{"key":"2026020213173600000_R3","first-page":"1906","volume-title":"Infect. 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