Proteomic approaches to the study of papillomavirus–host interactions

The identification of interactions between viral and host cellular proteins has provided major insights into papillomavirus research, and these interactions are especially relevant to the role of papillomaviruses in the cancers with which they are associated. Recent advances in mass spectrometry technology and data processing now allow the systematic identification of such interactions. This has led to an improved understanding of the different pathologies associated with the many papillomavirus types, and the diverse nature of these viruses is reflected in the spectrum of interactions with host proteins. Here we review a history of proteomic approaches, particularly as applied to the papillomaviruses, and summarize current techniques. Current proteomic studies on the papillomaviruses use yeast-two-hybrid or affinity purification-mass spectrometry approaches. We detail the advantages and disadvantages of each and describe current examples of papillomavirus proteomic studies, with a particular focus on the HPV E6 and E7 oncoproteins.

► Papillomavirus proteins engage in key interactions with host cell proteins.
► Affinity purification-mass spectrometry and yeast-two-hybrid are current strategies.
► Published proteomic studies have focused on the HPV E6 and E7 oncoproteins.
► HPV diversity and disease association are reflected by protein–protein interactions.