Impact of amino acid substitutions in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 on viral neutralization susceptibility to broadly neutralizing antibodies specific for the CD4 binding site

Table 2 PNLG sites at positions 301, 339, 386 and 392 of gp120 in 32 AE-Env clones

^aThe potential N-linked glycosylation (PNLG) sites at amino acid positions 301 (N301), 339 (N339), 386 (N386) and 392 (N392) were present or absent in the wild type of 32 AE-Env clones and HXB2. Amino acid sequences were aligned using the ClustalW algorithm with slight manual adjustment, followed by examining the potential N-linked glycosylation (PNLG) site using N-Glycosite (http://www.hiv.lanl.gov). PNLG sites are shown in bold text, while (-) represents a gap. Amino acid numbering is based on the HXB2 Env gp120.
^bFifteen AE-Env clones, 29CC1, 45PB1, 45CC1, 47PL1, 55PL1, 62PL1, 65CC4, 99PB2, 99CC8, 101PL1, 102CC2, 105PB1, 105PL2, 105PL3 and 107CC2 became b12 susceptible after removing PNLG sites, N186 and/or N197, whereas 17 AE-Env clones, 21PL2, 22PL1, 41PB3, 41CC1, 47CC11, 50PB2, 50PL1, 52PB3, 52PL4, 52PL7, 60PB2, 60PL2, 60CC3, 98CC2, 98CC3, 99PL2 and 104PB4, were b12 resistant after removing N186 and/or N197.

ISSN: 1742-4690