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Antibodies produced by Advanced Product Enterprises, and used in AIDS research, funded by IAVI (The International AIDS Vaccine Initiative), results in publication in the Journal of Virology.

Title:

Dissecting the neutralizing antibody specificities of broadly neutralizing sera from HIV-1 infected donors

Authors:

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, and Dennis R. Burton

Abstract:

Attempts to elicit broadly neutralizing antibody responses by 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 serum 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 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 SIV and HIV-2 viruses displaying highly conserved gp41 neutralizing epitopes, suggesting 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 capacity of the gp120-depleted samples was compared to 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 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.

Click here to get the article from JVI.

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