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Chomont N., Hocini H., Gody J. C., Bouhlal H., Becquart Pierre, Krief Bouillet C., Kazatchkine M., Belec L. Neutralizing monoclonal antibodies to human immunodeficiency virus type 1 do not inhibit viral transcytosis through mucosal epithelial cells. Virology, 2007, 370 (2), p. 246-254.

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Lien direct chez l'éditeur doi:10.1016/j.virol.2007.09.006

TitreNeutralizing monoclonal antibodies to human immunodeficiency virus type 1 do not inhibit viral transcytosis through mucosal epithelial cells
Année de publication2007
Type de documentArticle
AuteursChomont N., Hocini H., Gody J. C., Bouhlal H., Becquart Pierre, Krief Bouillet C., Kazatchkine M., Belec L.
SourceVirology, 2007, 370 (2), p. 246-254.
RésuméHIV-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.
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