Proteomic approaches to the study of papillomavirus–host interactions

Department of Microbiology and Immunobiology, Harvard Medical School, NRB Room 950, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. Electronic address: .
Virology (Impact Factor: 3.32). 01/2013; 435(1):57-69. DOI: 10.1016/j.virol.2012.09.046
Source: PubMed


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.

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Available from: Elizabeth A White, Jan 07, 2014
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    • "Thus, E6 affects the repair system, leading to the accumulation of DNA lesions (Araldi et al., 2013). E7 promotes the phosphorylation of retinoblastoma protein (pRb), leading to S phase entry (White and Howley, 2013), and is related to centrosome duplication and numeric aberrations (Duensing et al., 2000). The combined action of oncoproteins E5, E6, and E7 leads to genomic instability and malignancy (Araldi et al., 2013a; Araldi et al., 2015b). "
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