Structural analysis of human respiratory syncytial virus P protein: identification of intrinsically disordered domains

• Autor(a) principal: Simabuco,Fernando M
• Data de Publicação: 2011
• Outros Autores: Asara,John M, Guerrero,Manuel C, Libermann,Towia A, Zerbini,Luiz F, Ventura,Armando M
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Brazilian Journal of Microbiology
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000100043
• topic: Human respiratory syncytial virus; P protein; intrinsically disordered domains; oligomerization

Human Respiratory Syncytial Virus P protein plus the viral RNA, N and L viral proteins, constitute the viral replication complex. In this report we describe that HRSV P protein has putative intrinsically disordered domains predicted by in silico methods. These two domains, located at the amino and caboxi terminus, were identified by mass spectrometry analysis of peptides obtained from degradation fragments observed in purified P protein expressed in bacteria. The degradation is not occurring at the central oligomerization domain, since we also demonstrate that the purified fragments are able to oligomerize, similarly to the protein expressed in cells infected by HRSV. Disordered domains can play a role in protein interaction, and the present data contribute to the comprehension of HRSV P protein interactions in the viral replication complex.