ChomontN.auteurautHociniH.auteurautGodyJ. C.auteurautBouhlalH.auteurautBecquartPierreauteurautIRDKrief BouilletC.auteurautKazatchkineM.auteurautBelecL.auteurauttextjournalArticletext/pdfborn digitalaccessHIV-1 transcytosis has been proposed as a potential mechanism allowing the virus to cross the epithelium during mucosal transmission. Epitopes of the HIV-1 envelope involved in this process have not been identified yet. Here, we assessed a large panel of HIV neutralizing antibodies recognizing well-characterized epitopes of the HIV-1 envelope for their ability to block HIV-1 transcytosis across a confluent epithelial monolayer. We found that all of the 13 HIV-1-specific monoclonal antibodies tested in the present study, including the three broadly neutralizing antibodies 2F5. 2G12 and lgG1bI2, lacked the ability to inhibit transcytosis of cell-free and cell-associated R5- as X4-tropic HIV-1 across a tight and polarized monolayer of HEC-1 epithelial cells. In contrast, anti-gp 160 polyclonal antibodies purified from serum or breast milk of HIV-1-infected individuals potently inhibited HIV-1 transcytosis. Furthermore, polymeric S-IgA exhibited similar ability to inhibit transcytosis compared to IgG despite their lower anti-gp 160 specific activity. Together, these results demonstrate that the major neutralizing envelope epitopes of HIV-1 are not involved in HIV-1 transcytosis, and suggest that surface agglutination of virus particles may participate to the blocking effect observed with both polyclonal and polymeric anti-gp 160 immunoglobulins.specializedHIV 1HEC 1transcytosisneutralization052 370224625420070042-6822http://www.documentation.ird.fr/hor/fdi:01004089210.1016/j.virol.2007.09.006IRD BondyF B010040892http://www.documentation.ird.fr/hor/fdi:010040892http://www.documentation.ird.fr/intranet/publi/2008/01/010040892.pdfAccès réservé (Intranet de l'IRD)IRD - Base Horizon / Pleins textes2008-02-222010-08-04fdi:010040892<languageTerm authority="iso639-2b">fre</languageTerm>