| Full text | |
| Author(s): |
Simabuco, Fernando M.
[1]
;
Asara, John M.
[2]
;
Guerrero, Manuel C.
[2]
;
Libermann, Towia A.
[2]
;
Zerbini, Luiz F.
[2]
;
Ventura, Armando M.
[1]
Total Authors: 6
|
| Affiliation: | [1] Univ Sao Paulo, Dept Microbiol, Inst Ciencias Biomed, BR-05508900 Sao Paulo - Brazil
[2] Beth Israel Deaconess Med Ctr, Harvard Inst Med, Boston, MA 02215 - USA
Total Affiliations: 2
|
| Document type: | Journal article |
| Source: | Brazilian Journal of Microbiology; v. 42, n. 1, p. 340-345, JAN-MAR 2011. |
| Web of Science Citations: | 4 |
| Abstract | |
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. (AU) | |