Variability in the Glycosylation Patterns of gp120 Proteins from Different Human Immunodeficiency Virus Type 1 Isolates Expressed in Different Host Cells
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409, United States
Funder
National Cancer Institute
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
General Chemistry,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.1c00587
Reference78 articles.
1. The role of CD4 in HIV binding and entry
2. Human Immunodeficiency Virus (HIV) Envelope Binds to CXCR4 Independently of CD4, and Binding Can Be Enhanced by Interaction with Soluble CD4 or by HIV Envelope Deglycosylation
3. CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5
4. CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5
5. Sequential CD4-Coreceptor Interactions in Human Immunodeficiency Virus Type 1 Env Function: Soluble CD4 Activates Env for Coreceptor-Dependent Fusion and Reveals Blocking Activities of Antibodies against Cryptic Conserved Epitopes on gp120
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