The structure and host entry of an invertebrate parvovirus.
J Virol
; 87(23): 12523-30, 2013 Dec.
Article
em En
| MEDLINE
| ID: mdl-24027306
ABSTRACT
The 3.5-Å resolution X-ray crystal structure of mature cricket parvovirus (Acheta domesticus densovirus [AdDNV]) has been determined. Structural comparisons show that vertebrate and invertebrate parvoviruses have evolved independently, although there are common structural features among all parvovirus capsid proteins. It was shown that raising the temperature of the AdDNV particles caused a loss of their genomes. The structure of these emptied particles was determined by cryo-electron microscopy to 5.5-Å resolution, and the capsid structure was found to be the same as that for the full, mature virus except for the absence of the three ordered nucleotides observed in the crystal structure. The viral protein 1 (VP1) amino termini could be externalized without significant damage to the capsid. In vitro, this externalization of the VP1 amino termini is accompanied by the release of the viral genome.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Vírion
/
Parvovirus
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Infecções por Parvoviridae
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Internalização do Vírus
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Invertebrados
Limite:
Animals
/
Humans
Idioma:
En
Revista:
J Virol
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Estados Unidos