Email this article 
Proteins and microRNAs involved in papillomavirus infection
- Authors: Klimov EA1,2,3, Sobolev VV2,4,5, Solov’ev AM6, Perlamutrov Y.N6, Korsunskaya IM5
-
Affiliations:
- Lomonosov Moscow State University
- University Diagnostic Laboratory, LLC
- Center of Experimental Embryology and Reproductive Biotechnologies
- I.I. Mechnikov Research Institute for Vaccines and Sera
- Centre of Theoretical Problems of Physico-Chemical Pharmacology
- A.I. Yevdokimov Moscow State University of Medicine and Dentistry
- Issue: Vol 22, No 1 (2018)
- Pages: 43-49
- Section: IMMUNOLOGY. INFECTIOUS PATHOLOGY
- URL: https://journals.rudn.ru/medicine/article/view/18437
- DOI: https://doi.org/10.22363/2313-0245-2018-22-1-43-49
Cite item
Full Text
Abstract
The review is devoted to the analysis of proteins, protein complexes and microRNAs involved in papillomavirus infection. The papilloma viruses belong to the family of DNA-containing papovaviruses (Papovaviridae) and infect the basal layers of the epithelium. Human papillomaviruses (HPV) have an oncogenic potential, which varies significantly. The ring genome HPV encodes 6 early proteins and 2 later proteins (envelope proteins), and uses the host cell proteins for its own replication. For infection the membrane proteins that bind to the host cell membrane are especially important. In this paper we analyzed the arrays of literature data on proteins and microRNAs involved in binding, internalization, transport of HPV virions, and virus multiplication. The analysis of literature data was carried out using the program PathwayStudio9 ® and the database ResNet13 ® of Elsivier (USA), as well as online services. Total was revealed 69 infection-related proteins and protein complexes and 3 microRNAs (72 in total). As a result of the subsequent detailed analysis of the literature, 17 proteins and microRNAs involved in the following processes were selected: penetration of virus particles into the cell (7), transport of the virus in the cytoplasm of the host cell (5), transfer of the virus DNA into the core of the host cell (1) and regulation of gene transcription HPV (4). These proteins and microRNAs are potential targets for drugs that can prevent and suppress HPV infection.
Keywords
About the authors
E A Klimov
Lomonosov Moscow State University; University Diagnostic Laboratory, LLC; Center of Experimental Embryology and Reproductive Biotechnologies
Author for correspondence.
Email: klimov@mail.bio.msu.ru
-
V V Sobolev
University Diagnostic Laboratory, LLC; I.I. Mechnikov Research Institute for Vaccines and Sera; Centre of Theoretical Problems of Physico-Chemical Pharmacology
Email: klimov@mail.bio.msu.ru
A M Solov’ev
A.I. Yevdokimov Moscow State University of Medicine and Dentistry
Email: klimov@mail.bio.msu.ru
Yu N Perlamutrov
A.I. Yevdokimov Moscow State University of Medicine and Dentistry
Email: klimov@mail.bio.msu.ru
I M Korsunskaya
Centre of Theoretical Problems of Physico-Chemical Pharmacology
Email: klimov@mail.bio.msu.ru
References
- Munoz N, Bosch FX, de Sanjose S, et al. Epidemiologic classification of human papillomavirus types associated with cervical cancer. The New England journal of medicine. Feb 6 2003;348(6):518—527.
- de Villiers EM, Fauquet C, Broker TR, Bernard HU, zur Hausen H. Classification of papillomaviruses. Virology. Jun 20 2004;324(1):17—27.
- Stanley MA, Pett MR, Coleman N. HPV: from infection to cancer. Biochemical Society transactions. Dec 2007; 35(Pt 6):1456—1460.
- Cai Q, Lv L, Shao Q, Li X, Dian A. Human papillomavirus early proteins and apoptosis. Archives of gynecology and obstetrics. Mar 2013;287(3):541—548.
- Bellanger S, Tan CL, Nei W, He PP, Thierry F. The human papillomavirus type 18 E2 protein is a cell cycle-dependent target of the SCFSkp2 ubiquitin ligase. Journal of virology. Jan 2010;84(1):437—444.
- Doorbar J. The E4 protein; structure, function and patterns of expression. Virology. Oct 2013;445(1—2):80—98.
- Venuti A, Paolini F, Nasir L, et al. Papillomavirus E5: the smallest oncoprotein with many functions. Molecular cancer. 2011;10:140.
- Chung CH, Gillison ML. Human papillomavirus in head and neck cancer: its role in pathogenesis and clinical implications. Clinical cancer research : an official journal of the American Association for Cancer Research. Nov 15 2009;15(22):6758—6762.
- Zhou Q, Zhu K, Cheng H. Ubiquitination in host immune response to human papillomavirus infection. Archives of dermatological research. May 2011;303(4):217—230.
- Horvath CA, Boulet GA, Renoux VM, Delvenne PO, Bogers JP. Mechanisms of cell entry by human papillomaviruses: an overview // Virology journal. 2010;7:11.
- Aksoy P, Abban CY, Kiyashka E, Qiang W, Meneses PI. HPV16 infection of HaCaTs is dependent on beta4 integrin, and alpha6 integrin processing. Virology. Jan 20 2014; 449:45—52.
- Buck CB, Day PM, Thompson CD, et al. Human alpha-defensins block papillomavirus infection. Proceedings of the National Academy of Sciences of the United States of America. Jan 31 2006;103(5):1516—1521.
- Karanam B, Peng S, Li T, Buck C, Day PM, Roden RB. Papillomavirus infection requires gamma secretase. Journal of virology. Oct 2010;84(20):10661—10670.
- Wang X, Liu H, Ge H, et al. Viral DNA Replication Orientation and hnRNPs Regulate Transcription of the Human Papillomavirus 18 Late Promoter. mBio. May 30 2017;8(3).
- Mistry N, Drobni P, Naslund J, Sunkari VG, Jenssen H, Evander M. The anti-papillomavirus activity of human and bovine lactoferricin. Antiviral research. Sep 2007; 75(3):258—265.
- Drobni P, Naslund J, Evander M. Lactoferrin inhibits human papillomavirus binding and uptake in vitro. Antiviral research. Oct 2004;64(1):63—68.
- He J, Ji Y, Li A, et al. MiR-122 directly inhibits human papillomavirus E6 gene and enhances interferon signaling through blocking suppressor of cytokine signaling 1 in SiHa cells. PloS one. 2014;9(9):e108410.
- Nuovo GJ, Wu X, Volinia S, et al. Strong inverse correlation between microRNA-125b and human papillomavirus DNA in productive infection. Diagnostic molecular pathology : the American journal of surgical pathology, part B. Sep 2010;19(3):135—143.
- Day PM, Baker CC, Lowy DR, Schiller JT. Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression. Proceedings of the National Academy of Sciences of the United States of America. Sep 28 2004;101(39):14252—14257.
- Woodham AW, Da Silva DM, Skeate JG, et al. The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection. PloS one. 2012;7(8):e43519.
- Shafti-Keramat S, Handisurya A, Kriehuber E, Meneguzzi G, Slupetzky K, Kirnbauer R. Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses. Journal of virology. Dec 2003;77(24): 13125—13135.
- Bergant Marusic M, Ozbun MA, Campos SK, Myers MP, Banks L. Human papillomavirus L2 facilitates viral escape from late endosomes via sorting nexin 17. Traffic. Mar 2012;13(3):455—467.
- Ishii Y, Nakahara T, Kataoka M, et al. Identification of TRAPPC8 as a host factor required for human papillomavirus cell entry. PloS one. 2013;8(11):e80297.
- Broniarczyk J, Bergant M, Gozdzicka-Jozefiak A, Banks L. Human papillomavirus infection requires the TSG101 component of the ESCRT machinery. Virology. Jul 2014; 460—461:83—90.
