Our long-term goal is to understand basic processes involved in animal virus gene expression, including transcription, translation, and assembly of viral membranes. In addition, we are interested in basic questions about the potential usefulness of recombinant DNA technology in production of anti-viral vaccines. Four major areas of research are contemlated: We plan additional studies on transcription of the vesicular stomatitis virus (VSV) genome with emphasis on understanding the mechanisms which generate sequential mRNA transcription and localized transcription attenuation. We will continue our analysis of ribosome recognition of viral mRNA by determining if two """"""""extra"""""""" ribosome binding sites in a single viral mRNA species are actually used in vivo. We plan to use the VSV glycoprotein as a model system for understanding the assembly of viral and cellular membranes. These studies will focus on determination of protein sequence changes in mutant G proteins which are blocked at different stages of intracellular transport, and on the sequences of glycoproteins from different serotypes. Sequences will be determined from primers extended on the genomic RNA derived from G mutants. We will continue our studies on expression of the VSV glycoprotein in E. coli to determine if high level expression of the protein is possible, and if the protein produced is capable of inducing neutralizing antibody and immunity to viral infection in animals.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI015481-07
Application #
3126186
Study Section
Virology Study Section (VR)
Project Start
1979-01-01
Project End
1986-12-31
Budget Start
1985-01-01
Budget End
1985-12-31
Support Year
7
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Salk Institute for Biological Studies
Department
Type
DUNS #
005436803
City
La Jolla
State
CA
Country
United States
Zip Code
92037
Vahey, Maryanne T; Nau, Martin E; Taubman, Michele et al. (2003) Patterns of gene expression in peripheral blood mononuclear cells of rhesus macaques infected with SIVmac251 and exhibiting differential rates of disease progression. AIDS Res Hum Retroviruses 19:369-87
Doms, R W; Ruusala, A; Machamer, C et al. (1988) Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. J Cell Biol 107:89-99
Guan, J L; Cao, H; Rose, J K (1988) Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit. J Biol Chem 263:5306-13
Machamer, C E; Rose, J K (1988) Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane. J Biol Chem 263:5948-54
Machamer, C E; Rose, J K (1988) Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. J Biol Chem 263:5955-60
Rottier, P J; Florkiewicz, R Z; Shaw, A S et al. (1987) An internalized amino-terminal signal sequence retains full activity in vivo but not in vitro. J Biol Chem 262:8889-95
Machamer, C E; Rose, J K (1987) A specific transmembrane domain of a coronavirus E1 glycoprotein is required for its retention in the Golgi region. J Cell Biol 105:1205-14
Rottier, P J; Rose, J K (1987) Coronavirus E1 glycoprotein expressed from cloned cDNA localizes in the Golgi region. J Virol 61:2042-5
Kupfer, A; Kronebusch, P J; Rose, J K et al. (1987) A critical role for the polarization of membrane recycling in cell motility. Cell Motil Cytoskeleton 8:182-9
Puddington, L; Bevan, M J; Rose, J K et al. (1986) N protein is the predominant antigen recognized by vesicular stomatitis virus-specific cytotoxic T cells. J Virol 60:708-17

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