Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors.

Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. Research Abstract Details 

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Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. Abstract Text:

Amandeep K Dhillon,Helen Donners,Ralph Pantophlet,Welkin E Johnson,Julie M Decker,George M Shaw,Fang-Hua Lee,Douglas D Richman,Robert W Doms,Guido Vanham,Dennis R Burton,

Attempts to elicit broadly neutralizing antibody responses by human immunodeficiency virus type 1 (HIV-1) vaccine antigens have been met with limited success. To better understand the requirements for cross-neutralization of HIV-1, we have characterized the neutralizing antibody specificities present in the sera of three asymptomatic individuals exhibiting broad neutralization. Two individuals were infected with clade B viruses and the third with a clade A virus. The broadly neutralizing activity could be exclusively assigned to the protein A-reactive immunoglobulin G (IgG) fraction of all three donor sera. Neutralization inhibition assays performed with a panel of linear peptides corresponding to the third hypervariable (V3) loop of gp120 failed to inhibit serum neutralization of a panel of HIV-1 viruses. The sera also failed to neutralize chimeric simian immunodeficiency virus (SIV) and HIV-2 viruses displaying highly conserved gp41-neutralizing epitopes, suggesting that antibodies directed against these epitopes likely do not account for the broad neutralizing activity observed. Polyclonal IgG was fractionated on recombinant monomeric clade B gp120, and the neutralization capacities of the gp120-depleted samples were compared to that of the original polyclonal IgG. We found that the gp120-binding antibody population mediated neutralization of some isolates, but not all. Overall, the data suggest that broad neutralization results from more than one specificity in the sera but that the number of these specificities is likely small. The most likely epitope recognized by the monomeric gp120 binding neutralizing fraction is the CD4 binding site, although other epitopes, such as the glycan shield, cannot be excluded.

Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. Publishing Authors By Initials

AK Dhillon,H Donners,R Pantophlet,WE Johnson,JM Decker,GM Shaw,FH Lee,DD Richman,RW Doms,G Vanham,DR Burton,

For similar viruses: rna viruses: retroviridae: lentivirus: lentiviruses, primate: simian immunodeficiency virus research abstracts see: viruses: rna viruses: retroviridae: lentivirus: lentiviruses, primate: simian immunodeficiency virus research

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Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of virology

VOLUME: 81

Page Numbers: 6548-62

Journal Abbreviation: J. Virol.

ISSN: 0022-538X

DAY: 4

MONTH: 04

YEAR: 2007

Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 113724

Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. Keywords Mesh Terms:

KEYWORDS: Simian immunodeficiency virus

MESH TERMS: metabolism

Chemical & Substance for Abstract: Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. Information

Substance Name: Recombinant Proteins

Registry Number: 0

Grant and Affiliation Information for Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors.

AFFILIATION: The Scripps Research Institute, Department of Immunology (IMM-2), 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Country: United States

AGENCY: United States NIAID

GRANT: AI36214

ACRONYM: AI

MEDLINETA: J Virol

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