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Heparin enhances the furin cleavage of HIV‐1 gp160 peptides
Author(s) -
Pasquato A.,
Dettin M.,
Basak A.,
Gambaretto R.,
Tonin L.,
Seidah N.G.,
Di Bello C.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.050
Subject(s) - furin , cleavage (geology) , in vitro , heparin , human immunodeficiency virus (hiv) , gp41 , chemistry , biochemistry , peptide sequence , biology , virology , immunology , antigen , enzyme , gene , paleontology , fracture (geology) , epitope
Infectious HIV‐1 requires gp160 cleavage by furin at the REKR 511 ↓ motif ( site1 ) into the gp120/gp41 complex, whereas the KAKR 503 ( site2 ) sequence remains uncleaved. We synthesized 41mer and 51mer peptides, comprising site1 and site2 , to study their conformation and in vitro furin processing. We found that, while the previously reported 19mer and 13mer analogues represent excellent in vitro furin substrates, the present extended sequences require heparin for optimal processing. Our data support the hypothesis of a direct binding of heparin with site1 and site2 , allowing selective exposure/accessibility of the REKR sequence, which is only then optimally cleaved by furin.