N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10451/10690 |
Resumo: | © 2013 Elsevier B.V. All rights reserved. |
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N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranesHCVNS4BPhospholipidMembrane© 2013 Elsevier B.V. All rights reserved.HCV NS4B, a highly hydrophobic protein involved in the alteration of the intracellular host membranes forming the replication complex, plays a critical role in the HCV life cycle. NS4B is a multifunctional membrane protein that possesses different regions where diverse and significant functions are located. One of these important regions is the AH2 segment, which besides being highly conserved has been shown to play a significant role in NS4B functioning. We have carried out an in-depth biophysical study aimed at the elucidation of the capacity of this region to interact, modulate and disrupt membranes, as well as to study the structural and dynamic features relevant for that disruption. We show that a peptide derived from this region, NS4BAH2, is capable of specifically binding phosphatidyl inositol phosphates with high affinity, and its interfacial properties suggest that this segment could behave similarly to a pre-transmembrane domain partitioning into and interacting with the membrane depending on the membrane composition and/or other proteins. Moreover, NS4BAH2 is capable of rupturing membranes even at very low peptide-to-lipid ratios and its membrane-activity is modulated by lipid composition. NS4BAH2 is located in a shallow position in the membrane but it is able to affect the lipid environment from the membrane surface down to the hydrophobic core. The NS4B region where peptide NS4BAH2 resides might have an essential role in the membrane replication and/or assembly of the viral particle through the modulation of the membrane structure and hence the replication complex.This work was partially supported by grants REEQ/140/BIO/2005, PTDC/QUI-BIQ/114774/2009 and PTDC/QUI-BIQ/112929/2009 to M.R.B.C (FCT-MES, Portugal). H. N. is supported by a “Santiago Grisolía” fellowship from Generalitat Valenciana Autonomous Government, Spain. F.P.J. acknowledges FEBS for a Short Term Fellowship.ElsevierRepositório da Universidade de LisboaPalomares-Jerez, M. FranciscaNemesio, HenriqueFranquelim, Henri G.Castanho, Miguel A. R. B.Villalaín, José2014-03-06T11:17:20Z20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/10690engBiochimica et Biophysica Acta 1828 (2013) 1938–19520006-3002http://dx.doi.org/10.1016/j.bbamem.2013.04.020metadata only accessinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T15:56:21Zoai:repositorio.ul.pt:10451/10690Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:34:37.827361Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes |
title |
N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes |
spellingShingle |
N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes Palomares-Jerez, M. Francisca HCV NS4B Phospholipid Membrane |
title_short |
N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes |
title_full |
N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes |
title_fullStr |
N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes |
title_full_unstemmed |
N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes |
title_sort |
N-terminal AH2 segment of protein NS4B from hepatitis C virus : binding to and interaction with model biomembranes |
author |
Palomares-Jerez, M. Francisca |
author_facet |
Palomares-Jerez, M. Francisca Nemesio, Henrique Franquelim, Henri G. Castanho, Miguel A. R. B. Villalaín, José |
author_role |
author |
author2 |
Nemesio, Henrique Franquelim, Henri G. Castanho, Miguel A. R. B. Villalaín, José |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Repositório da Universidade de Lisboa |
dc.contributor.author.fl_str_mv |
Palomares-Jerez, M. Francisca Nemesio, Henrique Franquelim, Henri G. Castanho, Miguel A. R. B. Villalaín, José |
dc.subject.por.fl_str_mv |
HCV NS4B Phospholipid Membrane |
topic |
HCV NS4B Phospholipid Membrane |
description |
© 2013 Elsevier B.V. All rights reserved. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013 2013-01-01T00:00:00Z 2014-03-06T11:17:20Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10451/10690 |
url |
http://hdl.handle.net/10451/10690 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biochimica et Biophysica Acta 1828 (2013) 1938–1952 0006-3002 http://dx.doi.org/10.1016/j.bbamem.2013.04.020 |
dc.rights.driver.fl_str_mv |
metadata only access info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
metadata only access |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799134241548664832 |