Modification of human papillomavirus minor capsid protein L2 by sumoylation.
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.
Marusic
Martina Bergant
MB
University of Nova Gorica, Vipavska 13, SI-5000 Nova Gorica, Slovenia. martina.bergant@ung.si
Mencin
Nina
N
Licen
Mia
M
Banks
Lawrence
L
Grm
Helena Sterlinko
HS
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*
D036022:Capsid Proteins; C063316:L2 protein, Human papillomavirus type 16; D009856:Oncogene Proteins, Viral; D025842:SUMO-1 Protein; D008239:Lysine