Structural and Functional Properties of the Capsid Protein of Dengue and Related

Dengue virus (DENV) Flavivirus capsid protein (C protein) circular dichroism intrinsically disordered protein (IDP) protein–RNA interactions protein–host lipid systems interaction time-resolved fluorescence anisotropy

Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
08 Aug 2019
Historique:
received: 21 06 2019
revised: 05 08 2019
accepted: 06 08 2019
entrez: 11 8 2019
pubmed: 11 8 2019
medline: 15 1 2020
Statut: epublish

Résumé

Dengue, West Nile and Zika, closely related viruses of the Flaviviridae family, are an increasing global threat, due to the expansion of their mosquito vectors. They present a very similar viral particle with an outer lipid bilayer containing two viral proteins and, within it, the nucleocapsid core. This core is composed by the viral RNA complexed with multiple copies of the capsid protein, a crucial structural protein that mediates not only viral assembly, but also encapsidation, by interacting with host lipid systems. The capsid is a homodimeric protein that contains a disordered N-terminal region, an intermediate flexible fold section and a very stable conserved fold region. Since a better understanding of its structure can give light into its biological activity, here, first, we compared and analyzed relevant mosquito-borne

Identifiants

pubmed: 31398956
pii: ijms20163870
doi: 10.3390/ijms20163870
pmc: PMC6720645
pii:
doi:

Substances chimiques

Capsid Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Fundação para a Ciência e a Tecnologia
ID : Project PTDC/SAU-ENB/117013/2010
Organisme : Fundação para a Ciência e a Tecnologia
ID : Fellowship SFRH/BD/77609/2011
Organisme : Fundação para a Ciência e a Tecnologia
ID : Fellowship PD/BD/113698/2015
Organisme : Fundação para a Ciência e a Tecnologia
ID : Fellowship SFRH/BD/95856/2013
Organisme : Fundação Calouste Gulbenkian
ID : Project Science Frontiers Research Prize 2010
Organisme : Fundação para a Ciência e a Tecnologia
ID : Program Investigador FCT (IF/00772/2013)
Organisme : Fundação para a Ciência e a Tecnologia
ID : Program Concurso de Estímulo ao Emprego Científico (CEECIND/01670/2017)
Organisme : Fundação para a Ciência e a Tecnologia
ID : Project UID/BIM/50005/2019, Fundos do Orçamento do Estado

Déclaration de conflit d'intérêts

The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, and in the decision to publish the results.

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Auteurs

André F Faustino (AF)

Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.

Ana S Martins (AS)

Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.

Nina Karguth (N)

Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.

Vanessa Artilheiro (V)

Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.

Francisco J Enguita (FJ)

Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.

Joana C Ricardo (JC)

Centro de Química-Física Molecular, Instituto Superior Técnico, Universidade de Lisboa, 1049-001 Lisbon, Portugal.

Nuno C Santos (NC)

Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal. nsantos@fm.ul.pt.

Ivo C Martins (IC)

Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal. ivomartins@fm.ul.pt.

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Classifications MeSH