Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function.
Virology
; 420(1): 51-65, 2011 Nov 10.
Article
em En
| MEDLINE
| ID: mdl-21920573
ABSTRACT
JC virus (JCV) encodes a small basic phosphoprotein from the late coding region called agnoprotein, which has been shown to play important regulatory roles in the viral replication cycle. In this study, we report that agnoprotein forms highly stable dimers and higher order oligomer complexes. This was confirmed by immunoblotting and mass spectrometry studies. These complexes are extremely resistant to strong denaturing agents, including urea and SDS. Central portion of the protein, amino acids spanning from 17 to 42 is important for dimer/oligomer formation. Removal of 17 to 42 aa region from the viral background severely affected the efficiency of the JCV replication. Extracts prepared from JCV-infected cells showed a double banding pattern for agnoprotein in vivo. Collectively, these findings suggest that agnoprotein forms functionally active homodimer/oligomer complexes and these may be important for its function during viral propagation and thus for the progression of PML.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Infecções Tumorais por Vírus
/
Vírus JC
/
Infecções por Polyomavirus
/
Proteínas Virais Reguladoras e Acessórias
Limite:
Humans
Idioma:
En
Revista:
Virology
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Estados Unidos