Heparin enhances the furin cleavage of HIV‐1 gp160 peptides

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...

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Detalles Bibliográficos
Autores principales: Pasquato, A., Dettin, M., Basak, A., Gambaretto, R., Tonin, L., Seidah, N.G., Di Bello, C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2007
Materias:
Short Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7125586/
https://www.ncbi.nlm.nih.gov/pubmed/18037384
http://dx.doi.org/10.1016/j.febslet.2007.11.050
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author Pasquato, A.
Dettin, M.
Basak, A.
Gambaretto, R.
Tonin, L.
Seidah, N.G.
Di Bello, C.
author_facet Pasquato, A.
Dettin, M.
Basak, A.
Gambaretto, R.
Tonin, L.
Seidah, N.G.
Di Bello, C.
author_sort Pasquato, A.
collection PubMed
description 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.
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spelling pubmed-71255862020-04-06 Heparin enhances the furin cleavage of HIV‐1 gp160 peptides Pasquato, A. Dettin, M. Basak, A. Gambaretto, R. Tonin, L. Seidah, N.G. Di Bello, C. FEBS Lett Short Communications 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. John Wiley and Sons Inc. 2007-12-22 2007-11-26 /pmc/articles/PMC7125586/ /pubmed/18037384 http://dx.doi.org/10.1016/j.febslet.2007.11.050 Text en FEBS Letters 581 (2007) 1873-3468 © 2015 Federation of European Biochemical Societies This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.
spellingShingle Short Communications
Pasquato, A.
Dettin, M.
Basak, A.
Gambaretto, R.
Tonin, L.
Seidah, N.G.
Di Bello, C.
Heparin enhances the furin cleavage of HIV‐1 gp160 peptides
title Heparin enhances the furin cleavage of HIV‐1 gp160 peptides
title_full Heparin enhances the furin cleavage of HIV‐1 gp160 peptides
title_fullStr Heparin enhances the furin cleavage of HIV‐1 gp160 peptides
title_full_unstemmed Heparin enhances the furin cleavage of HIV‐1 gp160 peptides
title_short Heparin enhances the furin cleavage of HIV‐1 gp160 peptides
title_sort heparin enhances the furin cleavage of hiv‐1 gp160 peptides
topic Short Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7125586/
https://www.ncbi.nlm.nih.gov/pubmed/18037384
http://dx.doi.org/10.1016/j.febslet.2007.11.050
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