Abstract

We are studying the detailed receptor requirements of a group of animal viruses known to utilize sialyloligosaccharides of glycoproteins or glycolipids as host cell receptor determinants. These include influenza viruses, paramyxoviruses, polyoma virus and encephalomyocarditis virus. The interaction of these viruses with erythrocytes or cells in culture can be assessed by hemagglutination or infectivity, respectively. In either case, removal of cell surface sialic acids with neuraminidase prevents attachment of the virus. Sialyloligosaccharides of defined sequence can be introduced on the surface of the asialo-cells by reaction with purified sialyltransferases. By examining the ability of the sialyloligosaccharides elaborated by different sialyltransferases to restore viral hemagglutination to erythrocytes or viral infection to cultured cells, the receptor specificity of the virus can be defined. It is clear that these viruses can exhibit strict and varied specificities for sialyloligosaccharide receptors. Potential biological roles for viral receptor specificities in host selection will be explored.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI016165-07
Application #
3126579
Study Section
Virology Study Section (VR)
Project Start
1979-08-01
Project End
1987-07-31
Budget Start
1985-08-01
Budget End
1986-07-31
Support Year
7
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of California Los Angeles
Department
Type
Schools of Medicine
DUNS #
119132785
City
Los Angeles
State
CA
Country
United States
Zip Code
90095

  Publications

Leigh, M W; Connor, R J; Kelm, S et al. (1995) Receptor specificity of influenza virus influences severity of illness in ferrets. Vaccine 13:1468-73
Couceiro, J N; Baum, L G (1994) Characterization of the hemagglutinin receptor specificity and neuraminidase substrate specificity of clinical isolates of human influenza A viruses. Mem Inst Oswaldo Cruz 89:587-91
Couceiro, J N; Paulson, J C; Baum, L G (1993) Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium;the role of the host cell in selection of hemagglutinin receptor specificity. Virus Res 29:155-65
Kelm, S; Paulson, J C; Rose, U et al. (1992) Use of sialic acid analogues to define functional groups involved in binding to the influenza virus hemagglutinin. Eur J Biochem 205:147-53
Hanaoka, K; Pritchett, T J; Takasaki, S et al. (1989) 4-O-acetyl-N-acetylneuraminic acid in the N-linked carbohydrate structures of equine and guinea pig alpha 2-macroglobulins, potent inhibitors of influenza virus infection. J Biol Chem 264:9842-9
Pritchett, T J; Paulson, J C (1989) Basis for the potent inhibition of influenza virus infection by equine and guinea pig alpha 2-macroglobulin. J Biol Chem 264:9850-8
Suzuki, Y; Nagao, Y; Kato, H et al. (1987) The hemagglutinins of the human influenza viruses A and B recognize different receptor microdomains. Biochim Biophys Acta 903:417-24
Pritchett, T J; Brossmer, R; Rose, U et al. (1987) Recognition of monovalent sialosides by influenza virus H3 hemagglutinin. Virology 160:502-6
Rogers, G N; Herrler, G; Paulson, J C et al. (1986) Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J Biol Chem 261:5947-51
Anders, E M; Scalzo, A A; Rogers, G N et al. (1986) Relationship between mitogenic activity of influenza viruses and the receptor-binding specificity of their hemagglutinin molecules. J Virol 60:476-82

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