Premium
The N ‐linked glycan of the V3 region of HIV‐1 gp120 and CXCR4‐dependent multiplication of a human immunodeficiency virus type 1 lymphocyte‐tropic variant
Author(s) -
Losman Britt,
Biller Marlene,
Olofsson Sigvard,
Schønning Kristian,
Lund Ole Søgaard,
Svennerholm Bo,
Hansen John-Erik Stig,
Bolmstedt Anders
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00740-1
Subject(s) - virus , mutant , glycan , glycosylation , biology , virology , syncytium , infectivity , mutation , antibody , gp41 , permissive , wild type , microbiology and biotechnology , glycoprotein , genetics , gene , epitope
We have previously shown that an N ‐glycosylation site of N306 of HIV‐1 gp120 is not necessary for the HIV‐1 infectivity but protects HIV‐1 from neutralising antibodies. In contrast Nakayama et al. [FEBS Lett. (1998) 426, 367–372], using a virus with an identical V3 region, suggested that elimination of this particular glycan reduced the ability of T‐tropic HIV to bind to CXCR4 and hence its ability to infect T cell lines. We therefore re‐examined the ability of a mutant virus, lacking the N306 glycan, to replicate in various types of cells and found no change in co‐receptor usage for mutant virus. The ability of mutant virus to replicate or to induce syncytia in infected cells was similar to that of wild type virus. These results corroborate our original observation, confirming that the induced mutation in the N306 glycosylation site neither impairs nor improves the ability of mutant virus to replicate in permissive cells.