Otros
Unique structural features of flaviviruses’ capsid proteins: new insights on structure-function relationship
Fecha
2021-04-01Registro en:
Current Opinion in Virology, v. 47, p. 106-112.
1879-6265
1879-6257
10.1016/j.coviro.2021.02.005
2-s2.0-85102256124
Autor
Universidade Federal do Rio de Janeiro (UFRJ)
Universidade Estadual Paulista (Unesp)
Institución
Resumen
The Flaviviridae family comprises important human pathogens, including Dengue, Zika, West Nile, Yellow Fever and Japanese Encephalitis viruses. The viral genome, a positive-sense single-stranded RNA, is packaged by a single protein, the capsid protein, which is a small and highly basic protein that form intertwined homodimers in solution. Atomic-resolution structures of four flaviviruses capsid proteins were solved either in solution by nuclear magnetic resonance spectroscopy, or after protein crystallization by X-ray diffraction. Analyses of these structures revealed very particular properties, namely (i) the predominance of quaternary contacts maintaining the structure; (ii) a highly electropositive surface throughout the protein; and (iii) a flexible helix (α1). The goal of this review is to discuss the role of these features in protein structure-function relationship.