NDLI: Design of an Escherichia coli expressed HIV-1 gp120 fragment immunogen that binds to b12 and induces broad and potent neutralizing antibodies.

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Design of an Escherichia coli expressed HIV-1 gp120 fragment immunogen that binds to b12 and induces broad and potent neutralizing antibodies.

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Design of an Escherichia coli expressed HIV-1 gp120 fragment immunogen that binds to b12 and induces broad and potent neutralizing antibodies.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bhattacharyya, Sanchari Labranche, Celia C. Varadarajan, Raghavan Rathore, Ujjwal Purwar, Mansi Arendt, Heather Montefiori, David C. Phogat, Sanjay Wagner, Denise Singh, Pranveer Destefano, Joanne
Description	Author Affiliation: Bhattacharyya S ( Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.)
Abstract	b12, one of the few broadly neutralizing antibodies against HIV-1, binds to the CD4 binding site (CD4bs) on the gp120 subunit of HIV-1 Env. Two small fragments of HIV-1 gp120, b121a and b122a, which display about 70% of the b12 epitope and include solubility-enhancing mutations, were designed. Bacterially expressed b121a/b122a were partially folded and could bind b12 but not the CD4bs-directed non-neutralizing antibody b6. Sera from rabbits primed with b121a or b122a protein fragments and boosted with full-length gp120 showed broad neutralizing activity in a TZM-bl assay against a 16-virus panel that included nine Tier 2 and 3 viruses as well as in a five-virus panel previously designed to screen for broad neutralization. Using a mean IC50 cut-off of 50, sera from control rabbits immunized with gp120 alone neutralized only one virus of the 14 non-Tier 1 viruses tested (7%), whereas sera from b121a- and b122a-immunized rabbits neutralized seven (50%) and twelve (86%) viruses, respectively. Serum depletion studies confirmed that neutralization was gp120-directed and that sera from animals immunized with gp120 contained lower amounts of CD4bs-directed antibodies than corresponding sera from animals immunized with b121a/b122a. Competition binding assays with b12 also showed that b121a/2a sera contained significantly higher amounts of antibodies directed toward the CD4 binding site than the gp120 sera. The data demonstrate that it is possible to elicit broadly neutralizing sera against HIV-1 in small animals.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	14
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-04-05
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antibodies, Neutralizing Chemistry HIV Envelope Protein Gp120 Metabolism Amino Acid Sequence Animals Antigens, CD4 Binding Sites Binding, Competitive Biophysics Escherichia Coli Fluorescence Resonance Energy Transfer Immunoglobulin G Molecular Conformation Molecular Sequence Data Protein Binding Protein Conformation Proteins Rabbits Vaccines Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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