HIV-1 gp120 N-linked glycosylation differs between plasma and leukocyte compartments.

ABSTRACT:

Background

N-linked glycosylation is a major mechanism for minimizing virus neutralizing antibody response and is present on the Human Immunodeficiency Virus (HIV) envelope glycoprotein. Although it is known that glycosylation changes can dramatically influence virus recognition by the host antibody, the actual contribution of compartmental differences in N-linked glycosylation patterns remains unclear.

Methodology and principal findings

We amplified the env gp120 C2-V5 region and analyzed 305 clones derived from plasma and other compartments from 15 HIV-1 patients. Bioinformatics and Bayesian network analyses were used to examine N-linked glycosylation differences between compartments. We found evidence for cellspecific single amino acid changes particular to monocytes, and

SUBMITTER: Ho YS 

PROVIDER: S-EPMC2265691 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature