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PMID: 9600268 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Importance of the N-glycan in the V3 loop of HIV-1 envelope protein for CXCR-4- but not CCR-5-dependent fusion.

FEBS letters ·Vol. 426 ·No. 3 ·1998-04-24 ·Pages 367-72

Nakayama EE, Shioda T, Tatsumi M, Xin X, Yu D, Ohgimoto S, Kato A, Sakai Y, Ohnishi Y, Nagai Y

Abstract

The V3 region of HIV-1 envelope protein possesses a single N-linked sugar chain, which is conserved in most HIV-1 strains. We studied its role in the life cycle of HIV-1 strains with different co-receptor usage. Removal of the glycan appeared to cause a marked reduction of CXCR-4- but not CCR-5-dependent virus entry. A basic amino acid substitution at the 11th position of V3 markedly compensated for the removal of the N-glycan. These results indicate that the N-glycan plays an important role for CXCR-4-dependent virus entry and that this role is exerted in a particular context of the peptide backbone.

MeSH Terms
Amino Acid Sequence Amino Acid Substitution Cell Line, Transformed Giant Cells/virology Glycosylation HIV Envelope Protein gp120/genetics,metabolism HIV-1/isolation & purification,metabolism,physiology Humans Molecular Sequence Data Mutagenesis, Site-Directed Peptide Fragments/genetics,metabolism Polysaccharides/physiology Receptors, CCR5/physiology Receptors, CXCR4/physiology Receptors, HIV/physiology Virus Replication
Chemicals
HIV Envelope Protein gp120 HIV envelope protein gp120 (305-321) Peptide Fragments Polysaccharides Receptors, CCR5 Receptors, CXCR4 Receptors, HIV
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Nakayama E E
Department of Viral Infection, Institute of Medical Science, University of Tokyo, Japan.
Shioda T
Tatsumi M
Xin X
Yu D
Ohgimoto S
Kato A
Sakai Y
Ohnishi Y
Nagai Y
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1998-04-24
Pages
367-72
Language
English
Region
England
NLM ID
0155157
Subset
IM
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