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ArtigoDireito Autoral
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- IOC - Artigos de Periódicos [12500]
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COVID-2019: THE ROLE OF THE NSP2 AND NSP3 IN ITS PATHOGENESIS
Pandemia
Infecção
Patogênese
Análise de interação proteína-proteína
Métodos de pesquisa e análise
COVID-19
Coronavírus
Infection
Pandemics
Pathogeneseis
Protein-protein interaction analysis
Research and analysis methods
Em decorrência da pandemia decretada pela OMS em 2020, o artigo encontra-se em acesso aberto.
Autor(es)
Afiliação
University Campus Bio‐Medico of Rome. Unit of Clinical Laboratory Science. Rome, Italy.
University Campus Bio‐Medico of Rome. Unit of Medical Statistics and Molecular Epidemiology. Rome, Italy.
University of Rome “La Sapienza”. Department of Biochemical Sciences "A. Rossi Fanelli". Rome, Italy.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Flavivírus. Rio de Janeiro, RJ, Brasil.
University of Rome “La Sapienza”. Department of Biochemical Sciences "A. Rossi Fanelli". Rome, Italy.
University Campus Bio‐Medico of Rome. Unit of Medical Statistics and Molecular Epidemiology. Rome, Italy.
University Campus Bio‐Medico of Rome. Unit of Medical Statistics and Molecular Epidemiology. Rome, Italy.
University of Rome “La Sapienza”. Department of Biochemical Sciences "A. Rossi Fanelli". Rome, Italy.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Flavivírus. Rio de Janeiro, RJ, Brasil.
University of Rome “La Sapienza”. Department of Biochemical Sciences "A. Rossi Fanelli". Rome, Italy.
University Campus Bio‐Medico of Rome. Unit of Medical Statistics and Molecular Epidemiology. Rome, Italy.
Resumo em Inglês
Last December 2019, a new virus, named novel Coronavirus (COVID-2019) causing many cases of severe pneumonia was reported in Wuhan, China. The virus knowledge is limited and especially about COVID-2019 pathogenesis. The Open Reading Frame 1ab (ORF1ab) of COVID-2019 has been analyzed to evidence the presence of mutation caused by selective pressure on the virus. For selective pressure analysis fast-unconstrained Bayesian approximation (FUBAR) was used. Homology modelling has been performed by SwissModel and HHPred servers. The presence of transmembrane helical segments in Coronavirus ORF1ab non structural protein 2 (nsp2) and nsp3 was tested by TMHMM, MEMSAT, and MEMPACK tools. Three-dimensional structures have been analyzed and displayed using PyMOL. FUBAR analysis revealed the presence of potential sites under positive selective pressure (P < .05). Position 723 in the COVID-2019 has a serine instead a glycine residue, while at aminoacidic position 1010 a proline instead an isoleucine. Significant (P < .05) pervasive negative selection in 2416 sites (55%) was found. The positive selective pressure could account for some clinical features of this virus compared with severe acute respiratory syndrome (SARS) and Bat SARS-like CoV. The stabilizing mutation falling in the endosome-associated-protein-like domain of the nsp2 protein could account for COVID-2019 high ability of contagious, while the destabilizing mutation in nsp3 proteins could suggest a potential mechanism differentiating COVID-2019 from SARS. These data could be helpful for further investigation aimed to identify potential therapeutic targets or vaccine strategy, especially in the actual moment when the epidemic is ongoing and the scientific community is trying to enrich knowledge about this new viral pathogen.
Palavras-chave
EpidemiologiaPandemia
Infecção
Patogênese
Análise de interação proteína-proteína
Métodos de pesquisa e análise
COVID-19
Coronavírus
Palavras-chave em inglês
EpidemiologyInfection
Pandemics
Pathogeneseis
Protein-protein interaction analysis
Research and analysis methods
Editor
Wiley
Referência
ANGELETTI, Silvia et al. COVID‐2019: The role of the nsp2 and nsp3inits pathogenesis. Journal of Medical Virology, p. 1-5, 2020.DOI
10.1002/jmv.25719ISSN
0146-6615Notas
Devido a pandemia mundial do COVID-19, o artigo da revista foi liberado em acesso aberto durante o ano de 2020, visando divulgação e disseminação.Em decorrência da pandemia decretada pela OMS em 2020, o artigo encontra-se em acesso aberto.
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