Interaction of Human Immunodeficiency Virus (HIV) Glycans with Lectins of the Human Immune System

Author(s): Xin Ji, Ying Chen, Jonathan Faro, Henry Gewurz, James Bremer, Gregory T. Spear.

Journal Name: Current Protein & Peptide Science

Volume 7 , Issue 4 , 2006

Become EABM
Become Reviewer


Approximately half of the molecular mass of gp120, the receptor-binding envelope protein of human immunodeficiency virus (HIV), consists of N-linked glycans. Nearly half of these glycans are of the high mannose type. These high mannose glycans furnish a rich forest of mannose residues on the virus surface making HIV a prime target for interaction with mannose-specific lectins of the immune system. This review focuses on the known interactions between gp120 and immune system lectins some of which HIV appears to exploit. The effect of variation in glycosylation of gp120, especially with respect to clades of HIV, on binding of immune system lectins is highlighted.

Keywords: T helper cells, HIV envelope protein, gp41, histocompatibility complex (MHC), mannose receptor (MR)

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2006
Page: [317 - 324]
Pages: 8
DOI: 10.2174/138920306778017990
Price: $58

Article Metrics

PDF: 2