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4D9L

Fab structure of anti-HIV-1 gp120 V2 mAb 697

Summary for 4D9L
Entry DOI10.2210/pdb4d9l/pdb
DescriptorLight chain of Fab fragment of anti-HIV1 gp120 V2 mAb 697, Heavy chain of Fab fragment of anti-HIV1 gp120 V2 mAb 697 (3 entities in total)
Functional Keywordsig, antibody, hiv-1 gp120, immune system
Biological sourceHomo sapiens (human)
More
Total number of polymer chains8
Total formula weight185350.21
Authors
Pan, R.M.,Kong, X.P. (deposition date: 2012-01-11, release date: 2012-03-21, Last modification date: 2024-11-06)
Primary citationGorny, M.K.,Pan, R.,Williams, C.,Wang, X.H.,Volsky, B.,O'Neal, T.,Spurrier, B.,Sampson, J.M.,Li, L.,Seaman, M.S.,Kong, X.P.,Zolla-Pazner, S.
Functional and immunochemical cross-reactivity of V2-specific monoclonal antibodies from HIV-1-infected individuals.
Virology, 427:198-207, 2012
Cited by
PubMed Abstract: The recent analysis of the first successful RV144 vaccine trial revealed that a high titer of plasma anti-V2 antibodies (Abs) correlated with a decreased risk of HIV-1 infection in vaccine recipients. To understand the mechanism of immune correlates, we studied seven anti-V2 monoclonal Abs (mAbs) developed from HIV-1 infected individuals. The V2 mAbs target conserved epitopes, including the binding site for α4β7 integrin, and are broadly cross-reactive with various gp120 proteins. Preferential usage of the VH1-69 gene by V2 mAbs may depend on selection by the same antigenic structure. Six of seven V2 mAbs weakly neutralized four to eight of the 41 pseudoviruses tested and resistance to neutralization was correlated with longer V2 domains. The data suggest the presence of shared, conserved structural elements in the V2 loop, and these can be used in the design of vaccine immunogens inducing broadly reactive Abs with anti-viral activities.
PubMed: 22402248
DOI: 10.1016/j.virol.2012.02.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.485 Å)
Structure validation

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