{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T22:23:51Z","timestamp":1770503031456,"version":"3.49.0"},"reference-count":61,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2008,1,15]],"date-time":"2008-01-15T00:00:00Z","timestamp":1200355200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI49808"],"award-info":[{"award-number":["AI49808"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI49111"],"award-info":[{"award-number":["AI49111"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM46192"],"award-info":[{"award-number":["GM46192"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI33292"],"award-info":[{"award-number":["AI33292"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000245","name":"Michael Smith Foundation for Health Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000245","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2008,5]]},"abstract":"<jats:p>\n                    MAb 2G12 neutralizes HIV\u20101 by binding with high affinity to a cluster of high\u2010mannose oligosac charides on the envelope glycoprotein, gp120. Screening of phage\u2010displayed peptide libraries with 2G12 identified peptides that bind specifically, with\n                    <jats:italic>\n                      K\n                      <jats:sub>d<\/jats:sub>\n                      s\n                    <\/jats:italic>\n                    ranging from 0.4 to 200 \u03bcM. The crystal structure of a 21\u2010mer peptide ligand in complex with 2G12 Fab was determined at 2.8 \u00c5 resolution. Comparison of this structure with previous structures of 2G12\u2010carbohydrate complexes revealed striking differences in the mechanism of 2G12 binding to peptide\n                    <jats:italic>vs<\/jats:italic>\n                    . carbohy drate. The peptide occupies a site different from, but adjacent to, the primary carbohydrate\u2010binding site on 2G12, and makes only slightly fewer contacts to the Fab than Man\n                    <jats:sub>9<\/jats:sub>\n                    GlcNAc\n                    <jats:sub>2<\/jats:sub>\n                    (51\n                    <jats:italic>vs<\/jats:italic>\n                    . 56, respectively). However, only two antibody contacts with the peptide are hydro gen bonds in contrast to six with Man\n                    <jats:sub>9<\/jats:sub>\n                    GlcNAc\n                    <jats:sub>2<\/jats:sub>\n                    , and only three of the antibody residues that interact with Man\n                    <jats:sub>9<\/jats:sub>\n                    GlcNAc\n                    <jats:sub>2<\/jats:sub>\n                    also contact the peptide. Thus, this mechanism of peptide binding to 2G12 does not sup port structural mimicry of the native carbohydrate epitope on gp120, since it neither replicates the oligo saccharide footprint on the antibody nor most of the contact residues. Moreover, 2G12.1 peptide is not an immunogenic mimic of the 2G12 epitope, since anti sera produced against it did not bind gp120.\u2014Menendez, A., Calarese, D. A., Stanfield, R. L., Chow, K. C., Scanlan, C. N., Kunert, R., Katinger, H., Burton, D. R., Wilson, I. A., Scott, J. K. A peptide inhibitor of HIV\u20101 neutralizing antibody 2G12 is not a structural mimic of the natural carbohydrate epitope on gp120.\n                    <jats:italic>FASEB J<\/jats:italic>\n                    . 22, 1380\u20131392 (2008)\n                  <\/jats:p>","DOI":"10.1096\/fj.07-8983com","type":"journal-article","created":{"date-parts":[[2008,1,15]],"date-time":"2008-01-15T22:34:36Z","timestamp":1200436476000},"page":"1380-1392","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["A peptide inhibitor of HIV\u20101 neutralizing antibody 2G12 is not a structural mimic of the natural carbohydrate epitope on gp120"],"prefix":"10.1096","volume":"22","author":[{"given":"Alfredo","family":"Menendez","sequence":"first","affiliation":[{"name":"Department of Molecular Biology and Biochemistry Simon Fraser University Burnaby British Columbia Canada"},{"name":"A.M., Michael Smith Laboratories University of British Columbia Vancouver BC Canada"},{"name":"D.A.C., Center for the Study of Hepatitis C The Rockefeller University New York NY USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel A.","family":"Calarese","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology The Scripps Research Institute La Jolla California USA"},{"name":"A.M., Michael Smith Laboratories University of British Columbia Vancouver BC Canada"},{"name":"D.A.C., Center for the Study of Hepatitis C The Rockefeller University New York NY USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robyn L.","family":"Stanfield","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology The Scripps Research Institute La Jolla California USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keith C.","family":"Chow","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Biochemistry Simon Fraser University Burnaby British Columbia Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chris N.","family":"Scanlan","sequence":"additional","affiliation":[{"name":"Department of Immunology The Scripps Research Institute La Jolla California USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Renate","family":"Kunert","sequence":"additional","affiliation":[{"name":"Institute of Applied Microbiology University of Natural Resources and Applied Life Sciences Vienna Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Herman","family":"Katinger","sequence":"additional","affiliation":[{"name":"Institute of Applied Microbiology University of Natural Resources and Applied Life Sciences Vienna Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dennis R.","family":"Burton","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology The Scripps Research Institute La Jolla California USA"},{"name":"Department of Immunology The Scripps Research Institute La Jolla California USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ian A.","family":"Wilson","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology The Scripps Research Institute La Jolla California USA"},{"name":"The Skaggs Institute for Chemical Biology The Scripps Research Institute La Jolla California USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jamie K.","family":"Scott","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Biochemistry Simon Fraser University Burnaby British Columbia Canada"},{"name":"Faculty of Health Sciences Simon Fraser University Burnaby British Columbia Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,1,15]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.69.11.6609-6617.1995"},{"key":"e_1_2_6_3_1","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.1086\/516443","article-title":"Evaluation of monoclonal antibodies to human immunodeficiency virus type 1 primary isolates by neutralization assays: Performance criteria for selecting candidate antibodies for clinical trials","volume":"197","author":"D'Souza M. 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