AIDS and its dementia as a neuropeptide disorder: Role of VIP receptor blockade by human immunodeficiency virus envelope

1988 ◽  
Vol 23 (S1) ◽  
pp. S71-S73 ◽  
Author(s):  
Candace B. Pert ◽  
Craig C. Smith ◽  
Michael R. Ruff ◽  
Joanna M. Hill
Keyword(s):  
Human Immunodeficiency Virus ◽  
Receptor Blockade ◽  
Virus Envelope ◽  
Human Immunodeficiency Virus Envelope ◽  
Immunodeficiency Virus ◽  
Vip Receptor

Human immunodeficiency virus envelope glycoprotein 120 alters sleep and induces cytokine mRNA expression in rats

1996 ◽  
Vol 271 (2) ◽  
pp. 1-1 ◽  
Author(s):  
M. R. Opp ◽  
P. L. Rady ◽  
T. K. Hughes ◽  
P. Cadet ◽  
S. K. Tyring ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Mrna Expression ◽  
Envelope Glycoprotein ◽  
Cytokine Mrna ◽  
Virus Envelope ◽  
Cytokine Mrna Expression ◽  
Human Immunodeficiency Virus Envelope ◽  
Immunodeficiency Virus

Pages R963–R970: M. R. Opp, P. L. Rady, T. K. Hughes, Jr., P. Cadet, S. K. Tyring, and E. M. Smith. “Human immunodeficiency virus envelope glycoprotein 120 alters sleep and induces cytokine mRNA expression in rats.” On p. R968, Fig. 3 should appear as below. (See PDF)

scholarly journals Role of N-Linked Glycans in a Human Immunodeficiency Virus Envelope Glycoprotein: Effects on Protein Function and the Neutralizing Antibody Response

2002 ◽  
Vol 76 (9) ◽  
pp. 4199-4211 ◽  
Author(s):  
Miriam I. Quiñones-Kochs ◽  
Linda Buonocore ◽  
John K. Rose
Keyword(s):  
Human Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Protein Function ◽  
Neutralizing Antibodies ◽  
Immune Recognition ◽  
Wild Type ◽  
Virus Envelope ◽  
Mutant Proteins ◽  
Immunodeficiency Virus

ABSTRACT The envelope (Env) glycoprotein of human immunodeficiency virus (HIV) contains 24 N-glycosylation sites covering much of the protein surface. It has been proposed that one role of these carbohydrates is to form a shield that protects the virus from immune recognition. Strong evidence for such a role for glycosylation has been reported for simian immunodeficiency virus (SIV) mutants lacking glycans in the V1 region of Env (J. N. Reitter, R. E. Means, and R. C. Desrosiers, Nat. Med. 4:679-684, 1998). Here we used recombinant vesicular stomatitis viruses (VSVs) expressing HIV Env glycosylation mutants to determine if removal of carbohydrates in the V1 and V2 domains affected protein function and the generation of neutralizing antibodies in mice. Mutations that eliminated one to six of the sites for N-linked glycosylation in the V1 and V2 loops were introduced into a gene encoding the HIV type 1 primary isolate 89.6 envelope glycoprotein with its cytoplasmic domain replaced by that of the VSV G glycoprotein. The membrane fusion activities of the mutant proteins were studied in a syncytium induction assay. The transport and processing of the mutant proteins were studied with recombinant VSVs expressing mutant Env G proteins. We found that HIV Env V1 and V2 glycosylation mutants were no better than wild-type envelope at inducing antibodies neutralizing wild-type Env, although an Env mutant lacking glycans appeared somewhat more sensitive to neutralization by antibodies raised to mutant or wild-type Env. These results indicate significant differences between SIV and HIV with regard to the roles of glycans in the V1 and V2 domains.

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