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

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

Volume: 7 Issue: 4

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

Affiliation:

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

Abstract: 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.

Cite this article as:

Ji Xin, Chen Ying, Faro Jonathan, Gewurz Henry, Bremer James and T. Spear Gregory, Interaction of Human Immunodeficiency Virus (HIV) Glycans with Lectins of the Human Immune System, Current Protein & Peptide Science 2006; 7 (4) . https://dx.doi.org/10.2174/138920306778017990