Characterization of BIV Env core: implication for mechanism of BIV-mediated cell fusion.
Entry of lentiviruses, such as human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV), requires folding of two heptad repeat regions (HR1 and HR2) of gp41 into a trimer-of-hairpins, which subsequently brings virus and cell membrane into fusion. This motif is a generalized feature of viral fusion proteins and has been exploited in generating antiviral fusion agents. In the present paper, we report structural characters of Env protein from another lentivirus, bovine immunodeficiency virus (BIV), which contributes to a good animal model of HIV. BIV HR1 and HR2 regions are predicted by two different programs and expressed separately or conjointly in Escherichia coli. Biochemical and biophysical analyses show that the predicted HRs of BIV Env can form a stable trimer-of-hairpins or six-helix bundle just like that formed by feline immunodeficiency virus Env. Cell fusion assay demonstrates that the HR2 peptide of BIV can efficiently inhibit the virus-mediated cell fusion.
Li
Shu
S
Modern Virology Research Center, State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Zhu
Jieqing
J
Peng
Yu
Y
Cui
Shanshan
S
Wang
Chunping
C
Gao
George F
GF
Tien
Po
P
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002459:Cell Fusion; D002478:Cells, Cultured; D016087:Immunodeficiency Virus, Bovine / Q000502:physiology*; D008168:Lung / Q000166:cytology / Q000821:virology*; D008561:Membrane Fusion / Q000502:physiology*; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014759:Viral Envelope Proteins / Q000378:metabolism*; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000378:metabolism*
D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins
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