scholarly journals Critical role of Arg59 in the high-affinity gp120-binding region of CD4 for human immunodeficiency virus type 1 infection

Virology ◽  
2007 ◽  
Vol 363 (1) ◽  
pp. 69-78 ◽  
Author(s):  
Danielle Fontenot ◽  
Jason K. Jones ◽  
Mohammad M. Hossain ◽  
Pramod N. Nehete ◽  
Eric M. Vela ◽  
...  
2009 ◽  
Vol 90 (8) ◽  
pp. 1795-1805 ◽  
Author(s):  
Bizhan Romani ◽  
Susan Engelbrecht

Human immunodeficiency virus type 1 (HIV-1) viral protein R (Vpr) is an accessory protein that interacts with a number of cellular and viral proteins. The functions of many of these interactions in the pathogenesis of HIV-1 have been identified. Deletion of the vpr gene reduces the virulence of HIV-1 dramatically, indicating the importance of this protein for the virus. This review describes the current findings on several established functions of HIV-1 Vpr and some possible roles proposed for this protein. Because Vpr exploits cellular proteins and pathways to influence the biology of HIV-1, understanding the functions of Vpr usually involves the study of cellular pathways. Several functions of Vpr are attributed to the virion-incorporated protein, but some of them are attributed to the expression of Vpr in HIV-1-infected cells. The structure of Vpr may be key to understanding the variety of its interactions. Due to the critical role of Vpr in HIV-1 pathogenicity, study of the interactions between Vpr and cellular proteins may help us to understand the mechanism(s) of HIV-1 pathogenicity.


1996 ◽  
Vol 2 (4) ◽  
pp. 460-468 ◽  
Author(s):  
Michael Bukrinsky ◽  
Helena Schmidtmayerova ◽  
Gabriele Zybarth ◽  
Larisa Dubrovsky ◽  
Barbara Sherry ◽  
...  

1997 ◽  
Vol 71 (2) ◽  
pp. 1476-1484 ◽  
Author(s):  
J H Simon ◽  
P Stumbles ◽  
N Signoret ◽  
C Somoza ◽  
M Puklavec ◽  
...  

1993 ◽  
Vol 177 (4) ◽  
pp. 949-954 ◽  
Author(s):  
J H Simon ◽  
C Somoza ◽  
G A Schockmel ◽  
M Collin ◽  
S J Davis ◽  
...  

CD4 is the primary receptor for the human immunodeficiency virus type 1 (HIV-1). Early mutational studies implicated a number of residues of CD4, centered in the region 41-59, in binding to gp120. However, further mutational analyses, together with studies using inhibitory antibodies or CD4-derived peptides, have suggested that other regions of CD4 are also involved in binding or postbinding events during infection. To resolve these ambiguities, we used rat CD4 mutants in which particular regions were replaced with the corresponding sequence of human CD4. We have previously shown that some of these are able to bind HIV-1 gp120, and here we test their ability to act as functional receptors. We find that the presence of human CD4 residues 33-62 is enough to confer efficient receptor function to rat CD4, and we conclude that it is unlikely that regions of CD4 outside this sequence are involved in specific interactions with HIV-1 during either infection or syncytium formation.


Virology ◽  
2004 ◽  
Vol 328 (1) ◽  
pp. 89-100 ◽  
Author(s):  
Dineshkumar Thotala ◽  
Elizabeth A. Schafer ◽  
Biswanath Majumder ◽  
Michelle L. Janket ◽  
Marc Wagner ◽  
...  

1996 ◽  
Vol 40 (11) ◽  
pp. 827-835 ◽  
Author(s):  
Yukako Ohshiro ◽  
Tsutomu Murakami ◽  
Kazuhiro Matsuda ◽  
Kiyoshi Nishioka ◽  
Keiichi Yoshida ◽  
...  

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