Vesicular stomatitis virus and Newcastle disease virus are enveloped, RNA viruses which assemble at host cell plasma membrane. Mature virions are formed when regions of plasma membrane containing viral components bud from the cell. The project proposed is designed to explore some of the unresolved problems in the morphogenesis of these viruses. The goal of these studies is 1) to define the interactions of viral proteins in plasma membranes necessary for assembly and budding of the virus and 2) to characterize in detail the intracellular processing of viral glycoproteins. These studies include characterization of temperature sensitive mutants defective in assembly of virions.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
9R01GM037745-09
Application #
3293391
Study Section
Virology Study Section (VR)
Project Start
1986-04-01
Project End
1991-03-31
Budget Start
1986-04-01
Budget End
1987-03-31
Support Year
9
Fiscal Year
1986
Total Cost
Indirect Cost
Name
University of Massachusetts Medical School Worcester
Department
Type
Schools of Medicine
DUNS #
660735098
City
Worcester
State
MA
Country
United States
Zip Code
01655
McGinnes, Lori W; Reitter, Julie N; Gravel, Kathy et al. (2003) Evidence for mixed membrane topology of the newcastle disease virus fusion protein. J Virol 77:1951-63
McGinnes, L; Sergel, T; Reitter, J et al. (2001) Carbohydrate modifications of the NDV fusion protein heptad repeat domains influence maturation and fusion activity. Virology 283:332-42
McGinnes, L W; Sergel, T; Chen, H et al. (2001) Mutational analysis of the membrane proximal heptad repeat of the newcastle disease virus fusion protein. Virology 289:343-52
Sergel, T A; McGinnes, L W; Morrison, T G (2001) Mutations in the fusion peptide and adjacent heptad repeat inhibit folding or activity of the Newcastle disease virus fusion protein. J Virol 75:7934-43
Sergel, T A; McGinnes, L W; Morrison, T G (2000) A single amino acid change in the Newcastle disease virus fusion protein alters the requirement for HN protein in fusion. J Virol 74:5101-7
McGinnes, L W; Morrison, T G (1998) Role of carbohydrate processing and calnexin binding in the folding and activity of the HN protein of Newcastle disease virus. Virus Res 53:175-85
McGinnes, L W; Morrison, T G (1997) Disulfide bond formation is a determinant of glycosylation site usage in the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus. J Virol 71:3083-9
McGinnes, L W; Morrison, T G (1996) Role of cotranslational disulfide bond formation in the folding of the hemagglutinin-neuraminidase protein of Newcastle disease virus. Virology 224:465-76
Sergel, T; Morrison, T G (1995) Mutations in the cytoplasmic domain of the fusion glycoprotein of Newcastle disease virus depress syncytia formation. Virology 210:264-72
McGinnes, L W; Morrison, T G (1995) The role of individual oligosaccharide chains in the activities of the HN glycoprotein of Newcastle disease virus. Virology 212:398-410

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