한빛사논문
- 조회1,491
Abstract
Yang-Gyun Kim*
, Maneesha Muralinath$, Teresa Brandt$, Matthew Pearcy$, Kevin Hauns$, Ky Lowenhaupt*, Bertram L. Jacobs$¶||, and Alexander Rich*||
*Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Room 68-233, Cambridge, MA 02139-4307; $Graduate Program in Molecular and Cellular Biology, Arizona State University, Tempe, AZ 85287-2701; ¶Department of Microbiology, Arizona State University, Tempe, AZ 85287-2701; and Department of Biochemistry, College of Medicine, Chung-Ang University, 221 Heuksuk-dong, Dongjak-gu, Seoul 156-756, Korea
Abstract
The N-terminal domain of the E3L protein of vaccinia virus has sequence similarity to a family of Z-DNA binding proteins of defined three-dimensional structure and it is necessary for pathogenicity in mice. When other Z-DNA-binding domains are substituted for the similar E3L domain, the virus retains its lethality after intracranial inoculation. Mutations decreasing Z-DNA binding in the chimera correlate with decreases in viral pathogenicity, as do analogous mutations in wild-type E3L. A chimeric virus incorporating a related protein that does not bind Z-DNA is not pathogenic, but a mutation that creates Z-DNA binding makes a lethal virus. The ability to bind the Z conformation is thus essential to E3L activity. This finding may allow the design of a class of antiviral agents, including agents against variola (smallpox), which has an almost identical E3L.
Y.-G.K. and M.M. contributed equally to this work. ||To whom correspondence may be addressed.
논문정보
- Research article
- 2003년 05월 (BRIC 등록일 )
- 국내+국외 연구진
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