Structural and functional studies of the measles virus hemagglutinin: Identification of a novel site required for CD46 interaction

Virology

Volumn 256, Issue 1, 1999, Pages 142-151

  Patterson, John B ^a   Scheiflinger, Friedrich ^a   Manchester, Marianne ^a   Yilma, Tilahun ^b   Oldstone, Michael B A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; MEMBRANE COFACTOR PROTEIN; REGULATOR PROTEIN; VIRUS HEMAGGLUTININ;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATTLE PLAGUE VIRUS; CERCOPITHECIDAE; CHIMERA; CHO CELL; CONSENSUS SEQUENCE; ERYTHROCYTE; HEMAGGLUTINATION; HUMAN; HUMAN CELL; MEASLES VIRUS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION;

EID: 0033616528     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1999.9644     Document Type: Article

References (39)

1. Alkhatib G., Briedis D. J. The predicted primary structure of the measles virus hemagglutinin. Virology. 150:1986;479-490.
2. Bartz R., Brinckmann U., Dunster L., Rima B., Ter Meulen V., Schneider-Schaulies J. Mapping amino acids of the measles virus hemagglutinin responsible for receptor (CD46) downregulation. Virology. 224:1996;334-337.
3. Blain F., Liston P., Briedis D. J. The carboxy-terminal 18 amino acids of the measles virus hemagglutinin are essential for it biological function. Biochem. Biophys. Res. Commun. 214:1995;1232-1238.
4. Blixenkrone-Moller M., Bolt G., Dannemann Jensen T., Harder T., Svansson V. Comparative analysis of the attachment protein gene (H) of dolphin morbillivirus. Virus Res. 40:1996;47-56.
5. Buchholz C. J., Koller D., Devaux P., Mumenthaler C., Schneider-Schaulies J., Braun W., Gerlier D., Cattaneo R. Mapping of the primary binding site of measles virus to its receptor CD46. J. Biol. Chem. 272:1997;22072-22079.
6. Buckland R., Wild T. F. Is CD46 the cellular receptor for measles virus? Virus Res. 48:1997;1-9.
7. Cattaneo R., Rose J. K. Cell fusion by the envelope glycoprotein of persistent measles virus which caused lethal human brain disease. J. Virol. 67:1993;1493-1502.
8. Dorig R., Marcel A., Chopra A., Richardson C. D. The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell. 75:1993;295-305.
9. Fuerst T. R., Niles E. G., Studier F. W., Moss B. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA. 83:1986;8122-8126.
10. Gerald C., Buckland R., Barker R., Freeman G., Wild T. F. Measles virus haemagglutinin gene: Cloning, complete nucleotide sequence analysis and expression in COS cells. J. Gen. Virol. 67:1986;2695-2703.
11. Griffin D. E., Bellini W. J. Measles virus. Virology. 1996;Lippincott-Raven, Philadelphia. p. 1267-1312.
12. Hsu E. C., Dorig R. E., Sarangi F., Marcil A., Iorio C., Richardson C. D. Artificial mutations and natural variations in the CD46 molecules from human and monkey cells define regions important for measles virus binding. J. Virol. 71:1997;6144-6154.
13. Hsu E. C., Sarangi F., Iorio C., Sidhu M. S., Udem S. A., Dillehay D. L., Xu W., Rota P. A., Bellini W. J., Richardson C. D. A single amino acid change in the hemagglutinin protein of measles virus determines its ability to bind CD46 and reveals another receptor on marmoset B cells. J. Virol. 72:1998;2905-2916.
14. Hu A., Cattaneo R., Schwartz S., Norrby E. Role of N-linked oligosaccharide chains in the processing and antigenicity of measles virus haemagglutinin protein. J. Gen. Virol. 75:1994;2173-2181.
15. Hu A., Norrby E. Role of individual cysteine residues in the processing and antigenicity of the measles virus hemagglutinin protein. J. Gen. Virol. 75:1994;2173-2181.
16. Hummel B. K., Bellini W. J. Localization of antibody epitopes and functional domains in the hemagglutinin protein of measles virus. J. Virol. 69:1995;1913-1916.
17. Iwata K., Seya T., Yanagi Y., Pesando J., Johnson P., Okabe M., Ueda S., Ariga H., Nagasawa S. Diversity of sites for measles virus binding and for inactivation of complement C3b and C4b on membrane cofactor protein CD46. J. Biol. Chem. 270:1995;15148-15152.
18. Kovemees J., Blixenkrone-Moller M., Sharma B., Orvell C., Norrby E. The nucleotide sequence and deduced amino acid composition of the haemagglutinin and fusion proteins of the morbillivirus phocid distemper virus. J. Gen. Virol. 72:1991;2959-2966.
19. Kwong P. D., Wyatt R., Robinson J., Sweet R. W., Sodroski J., Hendrickson W. A. Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature. 393:1998;648-659.
20. Langedijk J. P., Daus F. J., van Oirschot J. T. Sequence and structure alignment of paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin. J. Virol. 71:1997;6155-6167.
21. Lecouturier V., Fayolle J., Caballero M., Carabana J., Celma M., Fernandez-Munoz R., Wild T., Buckland R. Identification of two amino acids in the hemagglutinin glycoprotein of measles virus (MV) that govern hemadsorption, HeLa cell fusion, and CD46 downregulation: Phenotypic markers that differentiate vaccine and wild-type MV strains. J. Virol. 70:1996;4200-4204.
22. Liszewski M. K., Post T. W., Atkinson J. P. Membrane cofactor protein (MCP or CD46): Newest member of the regulators of complement activation gene cluster. Annu. Rev. Immunol. 9:1991;431-455.
23. Malvoisin E., Wild T. F. Measles virus glycoproteins: Studies on the structure and interaction of the hemagglutinin and fusion proteins. J. Gen. Virol. 74:1993;2365-2372.
24. Manchester M., Gairin J. E., Patterson J. B., Alvarez J., Liszewski M. K., Eto D. S., Atkinson J. P., Oldstone M. B. A. Measles virus recognizes its receptor, CD46, via two distinct binding sites within SCR1-2. Virology. 233:1997;174-184.
25. Manchester M., Liszewski M. K., Atkinson J. P., Oldstone M. B. A. Multiple isoforms of CD46 (membrane cofactor protein) serve as receptors for measles virus. Proc. Natl. Acad. Sci. USA. 91:1994;2161-2165.
26. Manchester M., Valsamakis A., Kaufman R., Liszewski M. K., Atkinson J. P., Lublin D. M., Oldstone M. B. A. Measles virus and C3 binding sites are distinct on membrane cofactor protein (MCP; CD46). Proc. Natl. Acad. Sci. USA. 92:1995;2303-2307.
27. Naniche D., Varior-Krishnan G., Cervino F., Wild T. F., Rossi B., Rabourdin-Combe C., Gerlier D. Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus. J. Virol. 67:1993a;6025-6032.
28. Naniche D., Wild T. F., Rabourdin-Combe C., Gerlier D. Measles virus haemagglutinin induces down-regulation of gp57/67, a molecule involved in virus binding. J. Gen. Virol. 74:1993b;1073-1079.
29. Nussbaum O., Broder C. C., Moss B., Bar-Lev Stern L., Rozenblatt S., Berger E. A. Functional and structural interaction between measles virus hemagglutinin and CD46. J. Virol. 69:1995;3341-3349.
30. Oldstone M. B., Fujinami R. S., Lampert P. W. Membrane and cytoplasmic changes in virus-infected cells induced by interactions of antiviral anitbody with surface viral antigen. Prog. Med. Virol. 26:1980;45-93.
31. Oldstone M. B., Fujinami R. S., Tishon A., Finney D., Powell H. C., Lampert P. W. Mapping of the major histocompatibility complex and viral antigens on the plasma membrane of a measles virus-infected cell. Virology. 1983;426-437.
32. Richardson C., Hull D., Greer P., Hasel K., Berkovich A., Englund G., Bellini W., Rima B., Lazzarini R. The nucleotide sequence of the mRNA encoding the fusion protein of measles virus (Edmonston strain): A comparison of fusion proteins from several different paramyxoviruses. Virology. 155:1986;508-523.
33. Rima B. K., Earle J. A., Baczko K., ter Meulen V., Liebert U. G., Carstens C., Carabana J., Caballero M., Celma M. L., Fernandez-Munoz R. Sequence divergence of measles virus heamagglutinin during natural evolution and adaptation to cell culture. J. Gen. Virol. 78:1997;97-106.
34. Rota J. S., Hummel K. B., Rota P. A., Bellini W. J. Genetic variability of the glycoprotein genes of current wild-type measles isolates. Virology. 188:1992;135-142.
35. Sato T. A., Enami M., Kohama T. Isolation of measles virus hemagglutinin protein in a soluble form by protease digestion. J. Virol. 69:1995;513-516.
36. Sheshberadaran H., Norrby E. Characterization of epitopes on the measles virus hemagglutinin. Virology. 152:1986;58-65.
37. Shibahara K., Hotta H., Katayama Y., Homma M. Increased binding activity of measles virus to monkey red blood cells after long term passage in Vero cell cultures. J. Gen. Virol. 75:1994;3511-3516.
38. Wild T. F., Malvoisin E., Buckland R. Measles virus: Both the hemagglutinin and fusion glycoproteins are required for fusion. J. Gen. Virol. 72:1991;439-442.
39. Yamanaka M., Hsu D., Crisp T., Dale B., Grubman M., Yilma T. Cloning and sequence analysis of the hemagglutinin gene of the virulent strain of rinderpest virus. Virology. 166:1988;251-253.