2. Academic Validation
  3. The N-terminal conserved domain of rubella virus capsid interacts with the C-terminal region of cellular p32 and overexpression of p32 enhances the viral infectivity

The N-terminal conserved domain of rubella virus capsid interacts with the C-terminal region of cellular p32 and overexpression of p32 enhances the viral infectivity

  • Virus Res. 2002 May 10;85(2):151-61. doi: 10.1016/s0168-1702(02)00030-8.
Ketha V Krishna Mohan 1,  Berhane Ghebrehiwet,  Chintamani D Atreya
Affiliations

Affiliation

  • 1 Laboratory of Pediatric and Respiratory Viral diseases, Division of Viral Products, Section of Viral Pathogenesis and Adverse Reactions, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA.
PMID: 12034482 DOI: 10.1016/s0168-1702(02)00030-8
Abstract

Cellular 'defense collagens' are produced to launch virus-specific responses to clear the invading viruses. Cellular p32, the C1q binding protein is one such protein. In this report, we identified the interaction of p32 derived from a human lung diploid cell line (WI-38) with rubella virus capsid (RVCP from Therien strain) N-terminal 28-amino acid domain, which is conserved among several RV strains including the vaccine strains. We further identified that the C-terminal 69 aa of the mature p32 is sufficient to interact with the CP. In addition, we observed that in three independent Vero 76-derived cell lines constitutively overexpressing p32, the RV infectivity was enhanced. Our results suggest that RV has evolved a strategy whereby one of its proteins is recruited to interact with, and exploit the cellular defense machinery to its advantage.

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