title: Modification of human papillomavirus minor capsid protein L2 by sumoylation.
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.
authors.affiliation: University of Nova Gorica, Vipavska 13, SI-5000 Nova Gorica, Slovenia. martina.bergant@ung.si
authors.forename: Martina Bergant
authors.initials: MB
authors.lastname: Marusic
authors.forename: Nina
authors.initials: N
authors.lastname: Mencin
authors.forename: Mia
authors.initials: M
authors.lastname: Licen
authors.forename: Lawrence
authors.initials: L
authors.lastname: Banks
authors.forename: Helena Sterlinko
authors.initials: HS
authors.lastname: Grm
mesh_terms: D036022:Capsid Proteins / Q000378:metabolism*; D052162:Human papillomavirus 16 / Q000737:chemistry*; D006801:Humans; D008239:Lysine / Q000378:metabolism; D009856:Oncogene Proteins, Viral / Q000378:metabolism*; D011485:Protein Binding; D055550:Protein Stability; D025842:SUMO-1 Protein / Q000378:metabolism*
chemical_list: D036022:Capsid Proteins; C063316:L2 protein, Human papillomavirus type 16; D009856:Oncogene Proteins, Viral; D025842:SUMO-1 Protein; D008239:Lysine