A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding

被引:735
作者
Rizzuto, CD
Wyatt, R
Hernández-Ramos, N
Sun, Y
Kwong, PD
Hendrickson, WA
Sodroski, J [1 ]
机构
[1] Harvard Univ, Sch Med, Dept Pathol, Dana Farber Canc Inst,Dept Canc Immunol & AIDS, Boston, MA 02115 USA
[2] Columbia Univ, Howard Hughes Med Inst, Dept Biochem & Mol Biophys, New York, NY 10032 USA
[3] Harvard Univ, Sch Publ Hlth, Dept Immunol & Infect Dis, Boston, MA 02115 USA
关键词
D O I
10.1126/science.280.5371.1949
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The entry of primate immunodeficiency viruses into target cells depends on a sequential interaction of the gp120 envelope glycoprotein with the cellular receptors, CD4 and members of the chemokine receptor family. The gp120 third variable (V3) loop has been implicated in chemokine receptor binding, but the use of the CCR5 chemokine receptor by diverse primate immunodeficiency viruses suggests the involvement of an additional, conserved gp120 element. Through the use of gp120 mutants, a highly conserved gp120 structure was shown to be critical for CCR5 binding. This structure is located adjacent to the V3 loop and contains neutralization epitopes induced by CD4 binding. This conserved element may be a useful target for pharmacologic or prophylactic intervention in human immunodeficiency virus (HIV) infections.
引用
收藏
页码:1949 / 1953
页数:5
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