The structural characterization and antigenicity of the S protein of SARS-CoV / 基因组蛋白质组与生物信息学报·英文版
Genomics, Proteomics & Bioinformatics
; (4): 108-117, 2003.
Article
en En
| WPRIM
| ID: wpr-339516
Biblioteca responsable:
WPRO
ABSTRACT
The corona-like spikes or peplomers on the surface of the virion under electronic microscope are the most striking features of coronaviruses. The S (spike) protein is the largest structural protein, with 1,255 amino acids, in the viral genome. Its structure can be divided into three regions: a long N-terminal region in the exterior, a characteristic transmembrane (TM) region, and a short C-terminus in the interior of a virion. We detected fifteen substitutions of nucleotides by comparisons with the seventeen published SARS-CoV genome sequences, eight (53.3%) of which are non-synonymous mutations leading to amino acid alternations with predicted physiochemical changes. The possible antigenic determinants of the S protein are predicted, and the result is confirmed by ELISA (enzyme-linked immunosorbent assay) with synthesized peptides. Another profound finding is that three disulfide bonds are defined at the C-terminus with the N-terminus of the E (envelope) protein, based on the typical sequence and positions, thus establishing the structural connection with these two important structural proteins, if confirmed. Phylogenetic analysis reveals several conserved regions that might be potent drug targets.
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Filogenia
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Composición de Base
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Ensayo de Inmunoadsorción Enzimática
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Glicoproteínas de Membrana
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Datos de Secuencia Molecular
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Proteínas del Envoltorio Viral
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Secuencia de Aminoácidos
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Homología de Secuencia
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Análisis de Secuencia de ADN
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Estructura Terciaria de Proteína
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Genomics, Proteomics & Bioinformatics
Año:
2003
Tipo del documento:
Article