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- W2130565519 abstract "ABSTRACT The potential role of dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) binding in human immunodeficiency virus transmission across the mucosal barrier was investigated by assessing the ability of simian-human immunodeficiency chimeric viruses (SHIVs) showing varying degrees of mucosal transmissibility to bind the DC-SIGN expressed on the surface of transfected cells. We found that gp120 of the highly transmissible, pathogenic CCR5-tropic SHIV SF162P3 bound human and rhesus DC-SIGN with an efficiency threefold or greater than that of gp120 of the nonpathogenic, poorly transmissible parental SHIV SF162 , and this increase in binding to the DC-SIGN of the SHIV SF162P3 envelope gp120 translated into an enhancement of T-cell infection in trans . The presence of an additional glycan at the N-terminal base of the V2 loop of SHIV SF162P3 gp120 compared to that of the parental virus was shown to be responsible for the increase in binding to DC-SIGN. Interestingly, this glycan also conferred escape from autologous neutralization, raising the possibility that the modification occurred as a result of immune selection. Our data suggest that more-efficient binding of envelope gp120 to DC-SIGN could be relevant to the enhanced mucosal transmissibility of SHIV SF162P3 compared to that of parental SHIV SF162 ." @default.
- W2130565519 created "2016-06-24" @default.
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- W2130565519 date "2002-10-15" @default.
- W2130565519 modified "2023-10-09" @default.
- W2130565519 title "Addition of a Single gp120 Glycan Confers Increased Binding to Dendritic Cell-Specific ICAM-3-Grabbing Nonintegrin and Neutralization Escape to Human Immunodeficiency Virus Type 1" @default.
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- W2130565519 doi "https://doi.org/10.1128/jvi.76.20.10299-10306.2002" @default.
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