Host-virus specificity of morbilliviruses predicted by structural modeling of the marine mammal SLAM, a receptor

Comparative Immunology, Microbiology and Infectious Diseases

Volumn 33, Issue 3, 2010, Pages 227-241

  Ohishi, Kazue ^a   Ando, Akiko ^a,b   Suzuki, Rintaro ^c   Takishita, Kiyotaka ^a   Kawato, Masaru ^a   Katsumata, Etsuko ^d   Ohtsu, Dai ^e   Okutsu, Kenji ^e   Tokutake, Koji ^e   Miyahara, Hirokazu ^f   Nakamura, Hirotaka ^g   Murayama, Tsukasa ^b   Maruyama, Tadashi ^a  

^a JAPAN AGENCY FOR MARINE EARTH SCIENCE AND TECHNOLOGY   (Japan)

^b TOKAI UNIVERSITY   (Japan)

^c NATIONAL INSTITUTE OF AGROBIOLOGICAL SCIENCES   (Japan)

^d Kamogawa Sea World   (Japan)

^e Yokohama Hakkeijima Sea Paradise   (Japan)

^f Okinawa Churaumi Aquarium ^*  (Japan)

^g Kanazawa Zoo   (Japan)

Author keywords

Cetacean; Marine mammals; Morbillivirus; Pinniped; Signaling lymphocyte activation molecule (SLAM); Sirenian

Indexed keywords

CD150 ANTIGEN; COMPLEMENTARY DNA; IMMUNOGLOBULIN; VIRUS PROTEIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CANINE DISTEMPER MORBILLIVIRUS; CONTROLLED STUDY; DNA SEQUENCE; DOLPHIN; HOST RANGE; INFECTION RISK; KILLER WHALE; LEUKOCYTE; MEASLES VIRUS; MOLECULAR MODEL; MOLECULAR PHYLOGENY; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN PROTEIN INTERACTION; SEAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SIRENIA; SPECIES COMPARISON; VIRUS CELL INTERACTION;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, CD; CETACEA; DOGS; HEMAGGLUTININS, VIRAL; HOST-PATHOGEN INTERACTIONS; HUMANS; MODELS, BIOLOGICAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MORBILLIVIRUS; MORBILLIVIRUS INFECTIONS; PHYLOGENY; PINNIPEDIA; RECEPTORS, CELL SURFACE; SEQUENCE ANALYSIS, PROTEIN; SIRENIA; SPECIES SPECIFICITY; VIRUS ATTACHMENT;

ANIMALIA; CANINE DISTEMPER VIRUS; CANIS FAMILIARIS; CETACEA; MAMMALIA; MORBILLIVIRUS; PINNIPEDIA; SIRENIA;

EID: 77951024637     PISSN: 01479571     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cimid.2008.10.003     Document Type: Article

References (55)

1. Griffin D.E. Measles virus. Fields virology 2001, 1401-1441. Lippincott Williams & Wilkins, Philadelphia. 3rd ed. D.M. Knipe, P.M. Howley (Eds.).
2. Rweyemamu M., Roder P.L., Taylor W.P. Towards the global eradication of rinderpest. Rinderpest and Peste des Petis ruminants, virus plagues of large and small ruminants 2006, 298-322. Elsevier, [chapter 15]. T. Barrett, P.-P. Pastoret, W.P. Taylor (Eds.).
3. Normile D. Driven to extinction. Science 2008, 319:1606-1609.
4. Barrett T., Rima B.K. Molecular biology of morbillivirus diseases of marine mammals. Molecular and cell biology of marine mammals 2002, 161-172. Krieger Publishing Company, Malabar, Florida. C.J. Pfeiffer (Ed.).
5. Di Guardo G., Marruchella G., Agrimi U., Kennedy S. Morbillivirus infections in aquatic mammals: a brief overview. J Vet Med Ser A 2005, 52:88-93.
6. Cosby S.L., McQuaid S., Duffy N., Lyons C., Rima B.K., Allan G.M., et al. Characterization of a seal morbillivirus. Nature 1988, 336:115-116.
7. Kennedy S., Smyth J.A., McCullough S.J., Allan G.M., McNeilly F., McQuaid S. Confirmation of cause of recent seal deaths. Nature 1988, 335:404.
8. Osterhaus A.D., Vedder E.J. Identification of virus causing recent seal deaths. Nature 1988, 335:20.
9. Grachev M.A., Kumarev V.P., Mamaev L.V., Zorin V.L., Baranova L.V., Denikina N.N., et al. Distemper virus in Baikal seals. Nature 1989, 338:209.
10. Osterhaus A.D.M.E., Grosen J., Uytdehaag F.G.C.M., Visser I.K.G., van de Bildt M.W.G., Bergman A., et al. Distemper virus in Baikal seals. Nature 1989, 338:210.
11. Mamaev L.V., Visser I.K.G, Belikov S.I., Denikina N.N., Harder T., Goatley L., et al. Canine distemper virus in Lake Baikal seals (Phoca sibirica). Vet Rec 1996, 138:437-439.
12. Kennedy S., Smyth J.A., Cush P.F., McCullough S.J., Allan G.M., McQuaid S. Viral distemper now found in porpoises. Nature 1988, 336:21.
13. Domingo M., Ferrer L., Pumarola M., Marco A., Plana J., Kennedy S., et al. Morbillivirus in dolphins. Nature 1990, 348:21.
14. Lipscomb T.P., Schulman F.Y., Moffett D., Kennedy S. Morbilliviral disease in Atlantic bottle-nosed dolphins (Tursiops truncatus) from the 1987-1988 epizootic. J Wildl Dis 1994, 30:567-571.
15. Taubenberger J.K., Tsai M., Krafft A.E., Lichy J.H., Reid A.H., Schulman F.Y., et al. Two morbilliviruses implicated in bottlenose dolphin epizootics. Emerg Infect Dis 1996, 2:213-216.
16. Duignan P.J., House C., Walsh M.T., Campbell T., Bossart G.D., Duffy N., et al. Morbillivirus infection in manatees. Mar Mamm Sci 1995, 11:441-451.
17. Visser I.K.G., Kumarev V.P., Orvell C., de Vries P., Broeders H.W.J., van de Bildt M.W.J., et al. Comparison of two morbilliviruses isolated from seals during outbreaks of distemper in north west Europe and Siberia. Arch Virol 1990, 111:149-164.
18. Roelke-Parker M.E., Munson L., Packer C., Kock R., Cleaveland S., Carpenter M., et al. A canine distemper virus epidemic in Serengeti lions (Panthera leo). Nature 1996, 379:441-445.
19. Tatsuo H., Ono N., Tanaka K., Yanagi Y. SLAM (CDw150) is a cellular receptor for measles virus. Nature 2000, 406:893-897.
20. Tatsuo H., Ono N., Yanagi Y. Morbilliviruses use signaling lymphocyte activation molecules (CD150) as cellular receptors. J Virol 2001, 75:5842-5850.
21. Veillette A., Cruz-Munoz M., Zhong M. SLAM family receptors and SAP-related adaptors: matters arising. Trends Immunol 2006, 27:228-234.
22. Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., et al. The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM. Nature 1998, 395:462-469.
23. Sidorenko S.P., Clark E.A. Characterization of a cell surface glycoprotein IPO-3, expressed on activated human B and T lymphocytes. J Immunol 1993, 151:4614-4624.
24. Cocks B.G., Chang C.J., Carballido J.M., Yssel H., de Vries J.E., Aversa G. A novel receptor involved in T-cell activation. Nature 1995, 376:260-263.
25. Aversa G., Chang C.-C., Carballido J.M., Cocks B.G., de Vries J.E. Engagement of the signaling lymphocytic activation molecule (SLAM) on activated T cells results in IL-2-independent, cyclosporin A-sensitive T cell proliferation and IFN-gamma production. J Immunol 1997, 158:4036-4044.
26. Minagawa H., Tanaka K., Ono N., Tatsuo H., Yanagi Y. Induction of the measles virus receptor SLAM (CD150) on monocytes. J Gen Virol 2001, 82:2913-2917.
27. Bleharski J.R., Niazi K.R., Sieling P.A., Cheng G., Modlin R.L. Signaling lymphocytic activation molecule is expressed on CD40 ligand-activated dendritic cells and directly augments production of inflammatory cytokines. J Immunol 2001, 167:3174-3181.
28. Kruse M., Meinl E., Henning G., Kuhnt C., Berchtold S., Berger T., et al. Signaling lymphocyte activation molecule is expressed on mature CD83+ dendritic cells and is up-regulated by IL-1β. J Immunol 2001, 167:1989-1995.
29. Ohgimoto S., Ohgimoto K., Niewiesk S., Klagge I.M., Pfeuffer J., Johnston I.C.D., et al. The haemagglutinin protein is an important determinant of measles virus tropism for dendritic cells in vitro. J Gen Virol 2001, 82:1835-1844.
30. Mavaddat N., Mason D.W., Atkinson P.D., Evans E.J., Gilbert R.J., Stuart D.I., et al. Signaling lymphocytic activation molecule (CDw150) is homophilic but self-associates with very low affinity. J Biol Chem 2000, 275:28100-28109.
31. Sidorenko S.P., Clark E.A. The dual-function CD150 receptor subfamily: the viral attraction. Nat Immunol 2003, 4:19-24.
32. Ono N., Tatsuo H., Tanaka K., Minagawa H., Yanagi Y. V domain of human SLAM (CDw150) is essential for its function as a measles virus receptor. J Virol 2001, 75:1594-1600.
33. Ohno S., Seki F., Ono N., Yanagi Y. Histidine at position 61 and its adjacent amino acid residues are critical for the ability of SLAM (CD150) to act as a cellular receptor for measles virus. J GenVirol 2003, 84:2381-2388.
34. Xu Q., Zhang P., Hu C., Liu X., Qi Y., Liu Y. Identification of amino acid residues involved in the interaction between measles virus haemagglutin (MVH) and its human cell receptor (signaling lymphocyte activation molecule, SLAM). J Biochem Mol Biol 2006, 39:406-411.
35. Cao E., Ramagopal U.A., Fedorov A., Fedorov E., Yan Q., Lary J.W., et al. NTB-A receptor crystal structure: insights into homophilic interactions in the signaling lymphocytic activation molecule receptor family. Immunity 2006, 25:559-570.
36. Yan Q., Malashkevich V.N., Fedorov A., Fedorov E., Cao E., Lary J.W., et al. Structure of CD84 provides insight into SLAM family function. Proc Natl Acad Sci USA 2007, 104:10583-10588.
37. Guindon S., Gascuel O. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol 2003, 52:696-704.
38. Jones D.T., Taylor W.R., Thornton J.M. The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 1992, 8:275-282.
39. Ronquist F., Huelsenbeck J.P. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 2003, 19:1572-1574.
40. Bennett-Lovsey R.M., Herbert A.D., Sternberg M.J., Kelley L.A. Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 2008, 70:611-625.
41. Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
42. Fenn T.D., Ringe D., Petsko G.A. POVScript+: a program for model and data visualization using persistence of vision ray-tracing. J Appl Cryst 2003, 36:944-947.
43. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 1991, 24:946-950.
44. Murphy W.J., Eizirik E., O'Brien S.J., Madsen O., Scally M., Douady C.J., et al. Resolution of the early placental mammal radiation using Bayesian phylogenetics. Science 2001, 294:2348-2351.
45. Kriegs J.O., Churakov G., Kiefmann M., Jordan U., Brosius J., Schmitz J. Retroposed elements as archives for the evolutionary history of placental mammals. PLOS Biol 2006, 4:537-544.
46. Norrby E., Sheshberadaran H., McCullough K.C., Carpenter W.C., Orvell C. Is rinderpest virus the archevirus of the Morbillivirus genus?. Intervirology 1985, 23:228-232.
47. Dorig R.E., Marcil A., Chopra A., Richardson C.D. The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 1993, 75:295-305.
48. Naniche D., Varior-Krishnan G., Cervoni F., Wild T.F., Rossi B., Rabourdin-Combe C., et al. Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus. J Virol 1993, 67:6025-6032.
49. Bartz R., Brinckmann U., Dunster L.M., Rima B.K., ter Meulen V., Schneider-Schaulies J. Mapping amino acids of measles virus hemagglutinin responsible for receptor (CD46) downregulation. Virology 1996, 224:334-337.
50. Lecouturier V., Fayolle J., Caballero M., Carabana J., Celma M.L., Fernandez-Munoz R., et al. 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 1996, 70:4200-4204.
51. Hsu E.C., Sarangi F., Iorio C., Sidhu M.S., Udem S.A., Dillehay D.L., et al. 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 1998, 72:2905-2916.
52. Xie M.-F., Tanaka K., Ono N., Minagawa H., Yanagi Y. Amino acid substitutions at position 481 differently affect the ability of the measles virus hemagglutinin to induce cell fusion in monkey and marmoset cells co-expressing the fusion protein. Arch Virol 1999, 144:1689-1699.
53. Diallo A., Barrett T., Barbron M., Subbarao S.M., Taylor W.P. Differentiation of rinderpest and peste des petits ruminants viruses using specific cDNA clones. J Virol Methods 1989, 23:127-136.
54. Anderson E.C., Hassan A., Barrett T., Anderson J. Observations on the pathogenicity for sheep and goats and the transmissibility of the strain of virus isolated during the rinderpest outbreak in Sri Lanka in 1987. Vet Microbiol 1990, 21:309-318.
55. Blixenkrone-Moller M., Svansson V., Orvell C., Have P. Phocid distemper virus-a threat to terrestrial mammals?. Vet Rec 1990, 127:263-264.