Inhibition of HIV Infection by Lectin Binding to gp120 View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1997-09-23

AUTHORS

Jonathan M. Rhodes , Jeremy D. Milton , Theresa Animashaun , Naheed Mahmood

ABSTRACT

Human immunodeficiency virus (HIV) is the causative agent of AIDS (acquired immunodeficiency syndrome). The polypeptide precursor gp160 of HIV-1 forms the external glycoprotein, gp120 and the transmembrane glycoprotein, gp41 (1). Sequence variability is a feature of HIV viruses that have been classified into several subtypes (2). There are 22-31 potential N-linked glycosylation sites on gp120 depending on the HIV-1 isolate and thus, approximately half of its molecular weight is composed of carbohydrate. Gp120 oligosaccharides are a mixture of high mannose-, hybrid-, and complex-type N-glycans (3-5). The proportion of these N-glycan substituents on the envelope glycoprotein varies on different HIV-2 isolates propagated in different cell lines (6). The less-processed oligosaccharides are primarily located on conserved N-linked glycosylation sites on the recombinant gp120s produced in CHO cells and by a baculovirus expression system (4,7). This points to the high mannose and hybridtype oligosaccharides as being important in the structure and/or function of the envelope glycoprotein. More... »

PAGES

555-64

Book

TITLE

Lectin Methods and Protocols

ISBN

0-89603-396-1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1385/0-89603-396-1:555

DOI

http://dx.doi.org/10.1385/0-89603-396-1:555

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026135006

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21374492


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