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    Mannose-rich glycosylation patterns on HIV-1 subtype C gp120 and sensitivity to the lectins, Griffithsin, Cyanovirin-N and Scytovirin.

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    Journal article. (749.2Kb)
    Date
    2010
    Author
    Alexandre, Kabamba B.
    Gray, Elin S.
    Lambson, Bronwen E.
    Moore, Penny L.
    Choge, Isaac A.
    Mlisana, Koleka Patience.
    Abdool Karim, Salim Safurdeen.
    McMahon, James.
    O'Keefe, Barry.
    Chikwamba, Rachel.
    Morris, Lynn.
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    Abstract
    Griffithsin (GRFT), Cyanovirin-N (CV-N) and Scytovirin (SVN) are lectins that inhibit HIV-1 infection by binding to multiple mannose-rich glycans on the HIV-1 envelope glycoproteins (Env). Here we show that these lectins neutralize subtype C primary virus isolates in addition to Env-pseudotyped viruses obtained from plasma and cervical vaginal lavages. Among 15 subtype C pseudoviruses, the median IC50 values were 0.4, 1.8 and 20.1 nM for GRFT, CV-N and SVN, respectively, similar to what was found for subtype B and A. Analysis of Env sequences suggested that concomitant lack of glycans at positions 234 and 295 resulted in natural resistance to these compounds, which was confirmed by site-directed mutagenesis. Furthermore, the binding sites for these lectins overlapped that of the 2G12 monoclonal antibody epitope, which is generally absent on subtype C Env. This data support further research on these lectins as potential microbicides in the context of HIV-1 subtype C infection.
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    http://dx.doi.org/10.1016/j.virol.2010.03.021
    http://hdl.handle.net/10413/8042
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