Studies on Human Papillomavirus infectious entry

GARDIOL, D; BANKS, L; BUGNON VALDANO, MP

Workshop; NOVEL INSIGHTS ABOUT BACTERIAL AND VIRAL INFECTIONS - French-Argentine online meeting; 2019

Human Papillomaviruses (HPVs) are major human pathogens and the causative agents of a number of important human malignancies, with cervical cancer being the most important. The viruses replicate in differentiating epithelia, where the virus initially gains access to the basal cell compartment, which is thought to occur through microtraumas in the skin. The viral capsid contains the double-stranded viral genome of approximately 8 kb, which is enclosed by the viral coat proteins L1 and L2. Whilst both proteins play essential functions in capsid assembly and virus entry, the viral L2 protein appears to be the most important for ensuring delivery of the viral genome to the infected cell nucleus, where viral gene expression can initiate. The whole process of HPV infection involves multiple sequential steps, not all of which are well understood. The aim of this study is to identify new interacting partners and modifications of the minor capsid protein L2. Mass Spectrometry studies were done using purified HPV16 pseudovirions (PsV) produced in cultured cells led to the identification of CCT proteins as probable interaction partners of L2 HPV minor capsid protein. CCT, also known as TCP-1 Ring Complex or TRiC, is an essential and conserved chaperonin complex that interact with numerous cellular targets, assisting in their folding. In this study we analyze the interaction of HPV structural proteins with different components of the CCT complex and the relevance of this interaction during infection.