scholarly journals Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection.

1994 ◽  
Vol 91 (21) ◽  
pp. 9770-9774 ◽  
Author(s):  
C. T. Wild ◽  
D. C. Shugars ◽  
T. K. Greenwell ◽  
C. B. McDanal ◽  
T. J. Matthews
2007 ◽  
Vol 88 (11) ◽  
pp. 3139-3144 ◽  
Author(s):  
Yoshinao Kubo ◽  
Masaru Yokoyama ◽  
Hiroaki Yoshii ◽  
Chiho Mitani ◽  
Chika Tominaga ◽  
...  

CXCR4 functions as an infection receptor of X4 human immunodeficiency virus type 1 (HIV-1) . CXCR4 is glycosylated at the N-terminal extracellular region, which is important for viral envelope (Env) protein binding. We compared the effects of CXCR4 glycan on the CD4-dependent and –independent infections in human cells by X4 viruses. We found that transduction mediated by Env proteins of CD4-independent HIV-1 strains increased up to 5.5-fold in cells expressing unglycosylated CXCR4, suggesting that the CXCR4 glycan inhibits CD4-independent X4 virus infection. Co-expression of CD4 on the target cell surface or pre-incubation of virus particles with soluble CD4 abrogates the glycan-mediated inhibition of X4 virus infection, suggesting that interaction of Env protein with CD4 counteracts the inhibition. These findings indicate that it will be advantageous for X4 HIV-1 to remain CD4-dependent. A structural model that explains the glycan-mediated inhibition is discussed.


1998 ◽  
Vol 178 (3) ◽  
pp. 862-865 ◽  
Author(s):  
Maurizio de Martino ◽  
Chiara Azzari ◽  
Massimo Resti ◽  
Maria Moriondo ◽  
Maria Elisabetta Rossi ◽  
...  

2000 ◽  
Vol 61 (3) ◽  
pp. 347-351 ◽  
Author(s):  
Maurizio de Martino ◽  
Maria Moriondo ◽  
Chiara Azzari ◽  
Massimo Resti ◽  
Luisa Galli ◽  
...  

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