| Full text | |
| Author(s): |
Total Authors: 3
|
| Affiliation: | [1] Univ Sao Paulo, Sch Med Ribeirao Preto, Dept Cell Biol, BR-14049900 Sao Paulo, SP - Brazil
[2] Univ Fed Ouro Preto, Ouro Preto, MG - Brazil
[3] Univ Sao Paulo, Sch Med Ribeirao Preto, Virol Res Ctr, BR-14049900 Sao Paulo, SP - Brazil
Total Affiliations: 3
|
| Document type: | Journal article |
| Source: | VIROLOGY; v. 396, n. 2, p. 256-263, JAN 20 2010. |
| Web of Science Citations: | 9 |
| Abstract | |
Coxsackievirus B5 (CVB5), a human enterovirus of the family Picornaviridae, is a frequent cause of acute and chronic human diseases. The pathogenesis of enteroviral infections is not completely understood, and the fate of the CVB5-infected cell has a pivotal role in this process. We have investigated the CVB5-induced apoptosis of HeLa cells and found that it happens by the intrinsic pathway by a mechanism dependent on the ubiquitin-proteasome system, associated with nuclear aggregation of p53. Striking redistribution of both SUMO and UBC9 was noted at 4 h post-infection, simultaneously with a reduction in the levels of the ubiquitin-ligase HDM2. Taken together, these results suggest that CVB5 infection of HeLa cells elicit the intrinsic pathway of apoptosis by MDM2 degradation and p53 activation, destabilizing protein sumoylation, by a mechanism that is dependent on a functional ubiquitin-proteasome system. (C) 2009 Elsevier Inc. All rights reserved. (AU) | |