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

Brazilian Journal of Microbiology

Fernando M Simabuco²  John M Asara¹  Manuel C Guerrero¹  Towia A Libermann¹  Luiz F Zerbini¹  Armando M Ventura² 

[1] ,Universidade de São Paulo Instituto de Ciências Biomédicas Departamento de MicrobiologiaSão Paulo SP ,Brasil

关键词: Human respiratory syncytial virus;    P protein;    intrinsically disordered domains;    oligomerization;   

DOI  :  10.1590/S1517-83822011000100043

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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