Chomont N. auteur aut IRD Hocini H. auteur aut IRD Gody J. C. auteur aut IRD Bouhlal H. auteur aut IRD Becquart Pierre auteur aut IRD Krief Bouillet C. auteur aut IRD Kazatchkine M. auteur aut IRD Belec L. auteur aut IRD text journalArticle eng text/pdf reformatted digital access HIV-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. specialized HIV 1 HEC 1 transcytosis neutralization 052 370 2 246-254 2007 0042-6822 https://www.documentation.ird.fr/hor/fdi:010040892 10.1016/j.virol.2007.09.006 0042-6822 [F B010040892] https://www.documentation.ird.fr/hor/fdi:010040892 https://horizon.documentation.ird.fr/exl-doc/pleins_textes/2024-12/010040892.pdf IRD - Base Horizon / Pleins textes 2008-02-22 2024-12-24 fdi:010040892 fre