Abstract

We shall continue on the promising paths opened up by our research into the analysis of the two principal components of rhabdoviruses: the nucleocapsid genome and its polymerase enzymes, and the virion envelope (membrane) and its active components. We are investigating controls of VS viral transcription and replication. We will continue to examine the mechanisms by which VS virus interrupts cellular RNA synthesis, transport from the nucleus, processing, polyadenylation and polyribosome formation. We are continuing studies on temperature-sensitive mutants of VS virus and their pathogenicity and immunogenicity for mice. We are attempting to determine the lipid association of the matrix (M) protein by affinity labeling. Collaborative studies will continue with colleagues in the Biochemistry Department. We shall mount a frontal attack on the structure and function of viral membranes by use of refined chemical and biophysical techniques. These studies should elucidate the mechanisms of virus infection by membrane-membrane interaction and of virus budding.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
5R37AI011112-26
Application #
3480583
Study Section
Experimental Virology Study Section (EVR)
Project Start
1978-01-01
Project End
1992-12-31
Budget Start
1992-01-01
Budget End
1992-12-31
Support Year
26
Fiscal Year
1992
Total Cost
Indirect Cost

  Institution

Name
University of Virginia
Department
Type
Schools of Medicine
DUNS #
001910777
City
Charlottesville
State
VA
Country
United States
Zip Code
22904

  Publications

Grigera, P R; Garcia-Briones, M; Periolo, O et al. (1996) Immunogenicity of an aphthovirus chimera of the glycoprotein of vesicular stomatitis virus. J Virol 70:8492-501
Mathieu, M E; Grigera, P R; Helenius, A et al. (1996) Folding, unfolding, and refolding of the vesicular stomatitis virus glycoprotein. Biochemistry 35:4084-93
Ye, Z; Robinson, D; Wagner, R R (1995) Nucleus-targeting domain of the matrix protein (M1) of influenza virus. J Virol 69:1964-70
Justice, P A; Sun, W; Li, Y et al. (1995) Membrane vesiculation function and exocytosis of wild-type and mutant matrix proteins of vesicular stomatitis virus. J Virol 69:3156-60
Sun, W; Huang, L; Wagner, R R (1994) Common distribution of antigenic determinants and complementation activity on matrix proteins of two vesicular stomatitis virus serotypes. J Gen Virol 75 ( Pt 4):937-43
Suryanarayana, K; Baczko, K; ter Meulen, V et al. (1994) Transcription inhibition and other properties of matrix proteins expressed by M genes cloned from measles viruses and diseased human brain tissue. J Virol 68:1532-43
Ye, Z; Sun, W; Suryanarayana, K et al. (1994) Membrane-binding domains and cytopathogenesis of the matrix protein of vesicular stomatitis virus. J Virol 68:7386-96
Li, Y; Luo, L; Schubert, M et al. (1993) Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus. J Virol 67:4415-20
Ye, Z; Wagner, R R (1992) Down-regulation of vesicular stomatitis virus transcription by the matrix protein of influenza virus. J Gen Virol 73 ( Pt 3):743-8
Grigera, P R; Keil, W; Wagner, R R (1992) Disulfide-bonded discontinuous epitopes on the glycoprotein of vesicular stomatitis virus (New Jersey serotype). J Virol 66:3749-57

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