Characterization of BIV Env core: implication for mechanism of BIV-mediated cell fusion. Biochem Biophys Res Commun 2005 Apr 08;329(2):603-9
Date
03/02/2005Pubmed ID
15737628Pubmed Central ID
PMC7117376DOI
10.1016/j.bbrc.2005.01.160Scopus ID
2-s2.0-14644390292 (requires institutional sign-in at Scopus site) 3 CitationsAbstract
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.
Author List
Li S, Zhu J, Peng Y, Cui S, Wang C, Gao GF, Tien PAuthor
Jieqing Zhu PhD Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Binding Sites
Cattle
Cell Fusion
Cells, Cultured
Immunodeficiency Virus, Bovine
Lung
Membrane Fusion
Molecular Conformation
Molecular Sequence Data
Molecular Weight
Protein Binding
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Viral Envelope Proteins
Viral Fusion Proteins
