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
Research Project (R01)
Project #
5R01AI011112-20
Application #
3124891
Study Section
Experimental Virology Study Section (EVR)
Project Start
1978-01-01
Project End
1987-12-31
Budget Start
1986-01-01
Budget End
1986-12-31
Support Year
20
Fiscal Year
1986
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

Luo, L H; Li, Y; Snyder, R M et al. (1988) Point mutations in glycoprotein gene of vesicular stomatitis virus (New Jersey serotype) selected by resistance to neutralization by epitope-specific monoclonal antibodies. Virology 163:341-8
Li, Y; Luo, L Z; Snyder, R M et al. (1988) Site-specific mutations in vectors that express antigenic and temperature-sensitive phenotypes of the M gene of vesicular stomatitis virus. J Virol 62:3729-37
Shipley, J B; Pal, R; Wagner, R R (1988) Antigenicity, function, and conformation of synthetic oligopeptides corresponding to amino-terminal sequences of wild-type and mutant matrix proteins of vesicular stomatitis virus. J Virol 62:2569-77
Pal, R; Barenholz, Y; Wagner, R R (1988) Pyrene phospholipid as a biological fluorescent probe for studying fusion of virus membrane with liposomes. Biochemistry 27:30-6
Li, Y; Luo, L Z; Snyder, R M et al. (1988) Expression of the M gene of vesicular stomatitis virus cloned in various vaccinia virus vectors. J Virol 62:776-82
Baylor, N W; Li, Y; Ye, Z P et al. (1988) Transient expression and sequence of the matrix (M1) gene of WSN influenza A virus in a vaccinia vector. Virology 163:618-21
Ye, Z P; Pal, R; Fox, J W et al. (1987) Functional and antigenic domains of the matrix (M1) protein of influenza A virus. J Virol 61:239-46
Bricker, B J; Snyder, R M; Fox, J W et al. (1987) Monoclonal antibodies to the glycoprotein of vesicular stomatitis virus (New Jersey serotype): a method for preliminary mapping of epitopes. Virology 161:533-40
Pal, R; Barenholz, Y; Wagner, R R (1987) Vesicular stomatitis virus membrane proteins and their interactions with lipid bilayers. Biochim Biophys Acta 906:175-93
Ogden, J R; Pal, R; Wagner, R R (1986) Mapping regions of the matrix protein of vesicular stomatitis virus which bind to ribonucleocapsids, liposomes, and monoclonal antibodies. J Virol 58:860-8

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