Abstract

We are using membrane glycoproteins of envelopes viruses to investigate the mechanisms by which eurkaryotic cells direct proteins to various cellular compartments. Biochemical, genetic and recombinant DNA methods will be used to identify structural features of viral glycoproteins that determine their intracellular migration processes, and ultrastructural studies will be used to identify the cellular site at which glycoproteins are sorted into different membranes. We will further characterize the glycosylation sites and oligosaccharide chains of antigenic variants of influenza A viruses in an effort to understand the possible role of glycosylation in antigenic variation. Inhibitors of glycosylation will also be used to investigate the role of carbohydrates in the structure and biological and antigenic properities of the influenza A hemagglutinin glycoproteins. We will determine the primary structure of the glycoprotein of influenza C viruses, which differs from the hemagglutinin of influenza A and B viruses in structure and biological activities. The morphology of this glycoprotein and its arrangement on the viral envelope will be further investigated in electron microscopic studies.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI012680-12
Application #
3125249
Study Section
Virology Study Section (VR)
Project Start
1975-06-01
Project End
1987-06-30
Budget Start
1986-07-01
Budget End
1987-06-30
Support Year
12
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of Alabama Birmingham
Department
Type
School of Medicine & Dentistry
DUNS #
004514360
City
Birmingham
State
AL
Country
United States
Zip Code
35294

  Publications

Spiropoulou, C F; Goldsmith, C S; Shoemaker, T R et al. (2003) Sin Nombre virus glycoprotein trafficking. Virology 308:48-63
Ravkov, E V; Compans, R W (2001) Hantavirus nucleocapsid protein is expressed as a membrane-associated protein in the perinuclear region. J Virol 75:1808-15
Ravkov, E V; Nichol, S T; Peters, C J et al. (1998) Role of actin microfilaments in Black Creek Canal virus morphogenesis. J Virol 72:2865-70
Roberts, P C; Lamb, R A; Compans, R W (1998) The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation. Virology 240:127-37
Roberts, P C; Compans, R W (1998) Host cell dependence of viral morphology. Proc Natl Acad Sci U S A 95:5746-51
Yao, Q; Hu, X; Compans, R W (1997) Association of the parainfluenza virus fusion and hemagglutinin-neuraminidase glycoproteins on cell surfaces. J Virol 71:650-6
Blau, D M; Compans, R W (1997) Adaptation of measles virus to polarized epithelial cells: alterations in virus entry and release. Virology 231:281-9
Ravkov, E V; Nichol, S T; Compans, R W (1997) Polarized entry and release in epithelial cells of Black Creek Canal virus, a New World hantavirus. J Virol 71:1147-54
Huang, X F; Compans, R W; Chen, S et al. (1997) Polarized apical targeting directed by the signal/anchor region of simian virus 5 hemagglutinin-neuraminidase. J Biol Chem 272:27598-604
Yao, Q; Compans, R W (1996) Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection. Virology 223:103-12

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