Furin Cleavage of L2 during Papillomavirus Infection: Minimal Dependence on Cyclophilins.

ABSTRACT:

Unlabelled

Despite an abundance of evidence supporting an important role for the cleavage of minor capsid protein L2 by cellular furin, direct cleavage of capsid-associated L2 during human papillomavirus 16 (HPV16) infection remains poorly characterized. The conserved cleavage site, close to the L2 N terminus, confounds observation and quantification of the small cleavage product by SDS-PAGE. To overcome this difficulty, we increased the size shift by fusing a compact protein domain, the Propionibacterium shermanii transcarboxylase domain (PSTCD), to the N terminus of L2. The infectious PSTCD-L2 virus displayed an appreciable L2 size shift during infection of HaCaT keratinocytes. Cleavage under standard cell culture conditions rarely exceeded 35% of total L2. Cleavage levels were e

SUBMITTER: Bronnimann MP 

PROVIDER: S-EPMC4936150 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature