scholarly journals The immunodominance of epitopes within the transmembrane protein (gp41) of human immunodeficiency virus type 1 may be determined by the host's previous exposure to similar epitopes on unrelated antigens

1990 ◽  
Vol 71 (9) ◽  
pp. 1975-1983 ◽  
Author(s):  
D. Davis ◽  
B. Chaudhri ◽  
D. M. Stephens ◽  
C. A. Carne ◽  
C. Willers ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Transmembrane Protein ◽  
Previous Exposure ◽  
Immunodeficiency Virus ◽  
Protein Gp41

scholarly journals Peptides Corresponding to the Heptad Repeat Motifs in the Transmembrane Protein (gp41) of Human Immunodeficiency Virus Type 1 Elicit Antibodies to Receptor-Activated Conformations of the Envelope Glycoprotein

2001 ◽  
Vol 75 (18) ◽  
pp. 8859-8863 ◽  
Author(s):  
Eve de Rosny ◽  
Russell Vassell ◽  
Paul T. Wingfield ◽  
Carl T. Wild ◽  
Carol D. Weiss
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Transmembrane Protein ◽  
Heptad Repeat ◽  
Immunodeficiency Virus ◽  
Protein Gp41 ◽  
Hiv 1 ◽  
Bundle Structure

ABSTRACT Two heptad repeat regions in the ectodomain of the human immunodeficiency virus type 1 (HIV-1) transmembrane subunit (gp41) self-assemble into a six-helix bundle structure that is critical for virus entry. Immunizations with peptides corresponding to these regions generated antibodies specific to the receptor-activated conformations of gp41.

scholarly journals Structure-Function Studies of the Self-Assembly Domain of the Human Immunodeficiency Virus Type 1 Transmembrane Protein gp41

2000 ◽  
Vol 74 (11) ◽  
pp. 5368-5372 ◽  
Author(s):  
Yongkai Weng ◽  
Zhongning Yang ◽  
Carol D. Weiss
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Self Assembly ◽  
Transmembrane Protein ◽  
Helix Bundle ◽  
Immunodeficiency Virus ◽  
Protein Gp41 ◽  
Bundle Structure

ABSTRACT The coiled-coil region of the human immunodeficiency virus type 1 transmembrane protein (gp41) makes up the interior core of the six-helix bundle structure of the gp41 self-assembly domain. We extended our previous study of this domain (Y. Weng and C. D. Weiss, J. Virol. 72:9676–9682, 1998) by analyzing 23 additional mutants at positions that lie at the interface of the interior core and outer helices. We found nine new functional mutants. For most mutants, the activity could be explained by the ability of the modeled mutants to stabilize the six-helix bundle structure. The present study provides insights into the envelope glycoprotein fusion mechanism and information for rational drug and vaccine design.

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