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Aggregate complexes of HIV-1 induced by multimeric antibodies.

dc.contributor.author Denny, Thomas Norton
dc.contributor.author Ferrari, Guido
dc.contributor.author Haynes, Barton Ford
dc.contributor.author Hwang, KK
dc.contributor.author Kaewkungwal, J
dc.contributor.author Kim, JH
dc.contributor.author King, DF
dc.contributor.author Klein, Katja
dc.contributor.author Liu, P
dc.contributor.author Michael, NL
dc.contributor.author Montefiori, David Charles
dc.contributor.author Nitayaphan, Sorachai
dc.contributor.author Pitisuttithum, P
dc.contributor.author Rerks-Ngarm, S
dc.contributor.author Robb, ML
dc.contributor.author Shattock, RJ
dc.contributor.author Shen, X
dc.contributor.author Stieh, DJ
dc.contributor.author Tomaras, Georgia Doris
dc.coverage.spatial England
dc.date.accessioned 2017-06-01T19:10:31Z
dc.date.available 2017-06-01T19:10:31Z
dc.date.issued 2014-10-02
dc.identifier https://www.ncbi.nlm.nih.gov/pubmed/25274446
dc.identifier s12977-014-0078-8
dc.identifier.uri https://hdl.handle.net/10161/14673
dc.description.abstract BACKGROUND: Antibody mediated viral aggregation may impede viral transfer across mucosal surfaces by hindering viral movement in mucus, preventing transcytosis, or reducing inter-cellular penetration of epithelia thereby limiting access to susceptible mucosal CD4 T cells and dendritic cells. These functions may work together to provide effective immune exclusion of virus from mucosal tissue; however little is known about the antibody characteristics required to induce HIV aggregation. Such knowledge may be critical to the design of successful immunization strategies to facilitate viral immune exclusion at the mucosal portals of entry. RESULTS: The potential of neutralizing and non-neutralizing IgG and IgA monoclonals (mAbs) to induce HIV-1 aggregation was assessed by Dynamic light scattering (DLS). Although neutralizing and non-neutralizing IgG mAbs and polyclonal HIV-Ig efficiently aggregated soluble Env trimers, they were not capable of forming viral aggregates. In contrast, dimeric (but not monomeric) IgA mAbs induced stable viral aggregate populations that could be separated from uncomplexed virions. Epitope specificity influenced both the degree of aggregation and formation of higher order complexes by dIgA. IgA purified from serum of uninfected RV144 vaccine trial responders were able to efficiently opsonize viral particles in the absence of significant aggregation, reflective of monomeric IgA. CONCLUSIONS: These results collectively demonstrate that dIgA is capable of forming stable viral aggregates providing a plausible basis for testing the effectiveness of aggregation as a potential protection mechanism at the mucosal portals of viral entry.
dc.language eng
dc.relation.ispartof Retrovirology
dc.relation.isversionof 10.1186/s12977-014-0078-8
dc.subject Antibodies, Monoclonal
dc.subject HIV Antibodies
dc.subject HIV-1
dc.subject Humans
dc.subject Immunoglobulin A
dc.subject Immunoglobulin G
dc.title Aggregate complexes of HIV-1 induced by multimeric antibodies.
dc.type Journal article
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/25274446
pubs.begin-page 78
pubs.organisational-group Basic Science Departments
pubs.organisational-group Clinical Science Departments
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Duke Human Vaccine Institute
pubs.organisational-group Immunology
pubs.organisational-group Institutes and Centers
pubs.organisational-group Medicine
pubs.organisational-group Medicine, Duke Human Vaccine Institute
pubs.organisational-group Molecular Genetics and Microbiology
pubs.organisational-group School of Medicine
pubs.organisational-group Staff
pubs.organisational-group Surgery
pubs.organisational-group Surgery, Surgical Sciences
pubs.publication-status Published online
pubs.volume 11
dc.identifier.eissn 1742-4690


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