| Literature DB >> 15099755 |
David Opalka1, Antonello Pessi, Elisabetta Bianchi, Gennaro Ciliberto, William Schleif, Michael McElhaugh, Renee Danzeisen, Romas Geleziunas, Michael Miller, Debra M Eckert, David Bramhill, Joseph Joyce, James Cook, William Magilton, John Shiver, Emilio Emini, Mark T Esser.
Abstract
A fluorescence-based, multiplexed, antibody-binding and mapping assay was developed to characterize antibody responses in HIV-1-infected individuals to the ectodomain of the HIV-1 gp41 envelope glycoprotein. The antigen panel included intact recombinant gp41, the fusion peptide region, the polar region, the N-heptad region, the C-heptad region as well as overlapping epitopes in the 2F5 and 4E10 monoclonal antibody-binding regions. The panel included both native and constrained peptides specifically designed to mimic putative gp41 prefusion and fusion intermediates. The results of these analyses revealed a broad pattern of immune responses against the test antigens, suggesting that none of these gp41 regions are immunologically silent. The HIV-1-positive sera were also evaluated using infectivity inhibition assays. No correlation was evident between the breadth or magnitude of specific anti-gp41 reactivities and virus neutralization potency. These evaluations demonstrated the substantial potential of the multiplexed antibody binding and mapping assay for rapid and sensitive analysis of complex antibody responses.Entities:
Mesh:
Substances:
Year: 2004 PMID: 15099755 DOI: 10.1016/j.jim.2004.01.016
Source DB: PubMed Journal: J Immunol Methods ISSN: 0022-1759 Impact factor: 2.303