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Characterization of physical binding between human papillomavirus 18 protein E7 and centromere protein C.

Abstract
Human papillomaviruses (HPVs) have been linked to a variety of human diseases, most notably cancer of the cervix. In the majority of cases, HPV proteins E6 and E7 are continuously expressed and bind a variety of cellular proteins. The precise mechanism of HPV-induced carcinogenesis has not been fully elucidated; therefore, we attempted to identify the cellular proteins that interact with HPV18 E7 to better understand the function of this important protein. Using yeast 2-hybrid screening, we identified centromere protein C (CENP-C) as one of the proteins that interact with HPV18 E7. CENP-C interacted with E7 from HPV18 but not from HPV11. The CR2 domain of HPV18 E7 and the C-terminal region of CENP-C were found to be involved in the binding of these proteins. CENP-C is a component of the inner kinetochore and plays an essential role in proper chromosome segregation, mitotic checkpoint function, and kinetochore assembly. HPV18 E7-CENP-C binding may therefore impair centromere function, in turn causing cancers. We speculate that altered function of CENP-C as a result of interactions with HPV E7 may be associated with chromosomal abnormalities in HPV18-positive cancers.
AuthorsYuji Yaginuma, Kinya Yoda, Katsuhiro Ogawa
JournalOncology (Oncology) Vol. 79 Issue 3-4 Pg. 219-28 ( 2010) ISSN: 1423-0232 [Electronic] Switzerland
PMID21358210 (Publication Type: Journal Article)
CopyrightCopyright © 2011 S. Karger AG, Basel.
Chemical References
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • E7 protein, Human papillomavirus type 18
  • Oncogene Proteins, Viral
  • centromere protein C
Topics
  • Brain (metabolism)
  • Chromosomal Proteins, Non-Histone (genetics, metabolism)
  • DNA-Binding Proteins (genetics, metabolism)
  • Fetus (metabolism)
  • Gene Library
  • Humans
  • Immunoblotting
  • Immunoprecipitation
  • Oncogene Proteins, Viral (genetics, metabolism)
  • Protein Binding
  • Two-Hybrid System Techniques

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