| Literature DB >> 20739540 |
Martina Bergant Marusic1, Nina Mencin, Mia Licen, Lawrence Banks, Helena Sterlinko Grm.
Abstract
The human papillomavirus (HPV) minor capsid protein L2 plays important roles in the generation of infectious viral particles and in the initial steps of infection. Here we show that HPV-16 L2 protein is sumoylated at lysine 35 and that sumoylation affects its stability. Interestingly, the sumoylated form of L2 cannot bind to the major capsid protein L1, suggesting a mechanism by which capsid assembly may be modulated in an infected cell. Additionally, L2 appears to modulate the overall sumoylation status of the host cell. These observations indicate a complex interplay between the HPV L2 protein and the host sumoylation machinery.Entities:
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Year: 2010 PMID: 20739540 PMCID: PMC2953202 DOI: 10.1128/JVI.01269-10
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103