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Volumn 84, Issue 6, 2010, Pages 2753-2761

Canine distemper viruses expressing a hemagglutinin without N-glycans lose virulence but retain immunosuppression

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDASE; HEMAGGLUTININ;

EID: 77649140879     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01813-09     Document Type: Article
Times cited : (62)

References (55)
  • 1
    • 55249083109 scopus 로고    scopus 로고
    • The region between the canine distemper virus M and F genes modulates virulence by controlling fusion protein expression
    • Anderson, D. E., and V. von Messling. 2008. The region between the canine distemper virus M and F genes modulates virulence by controlling fusion protein expression. J. Virol. 82:10510-10518.
    • (2008) J. Virol , vol.82 , pp. 10510-10518
    • Anderson, D.E.1    von Messling, V.2
  • 2
    • 0029058912 scopus 로고
    • Individual roles of N-linked oligosaccharide chains in intracellular transport of the paramyxovirus SV5 fusion protein
    • Bagai, S., and R. A. Lamb. 1995. Individual roles of N-linked oligosaccharide chains in intracellular transport of the paramyxovirus SV5 fusion protein. Virology 209:250-256.
    • (1995) Virology , vol.209 , pp. 250-256
    • Bagai, S.1    Lamb, R.A.2
  • 3
    • 20044365620 scopus 로고    scopus 로고
    • Wild-type Rinderpest virus uses SLAM (CD150) as its receptor
    • Baron, M. D. 2005. Wild-type Rinderpest virus uses SLAM (CD150) as its receptor. J. Gen. Virol. 86:1753-1757.
    • (2005) J. Gen. Virol , vol.86 , pp. 1753-1757
    • Baron, M.D.1
  • 4
    • 0030273058 scopus 로고    scopus 로고
    • Mapping amino acids of measles virus hemagglutinin responsible for receptor (CD46) downregulation
    • Bartz, R., U. Brinckmann, L. M. Dunster, B. Rima, V. ter Meulen, and J. Schneider-Schaulies. 1996. Mapping amino acids of measles virus hemagglutinin responsible for receptor (CD46) downregulation. Virology 224:334-337.
    • (1996) Virology , vol.224 , pp. 334-337
    • Bartz, R.1    Brinckmann, U.2    Dunster, L.M.3    Rima, B.4    ter Meulen, V.5    Schneider-Schaulies, J.6
  • 5
    • 0019579733 scopus 로고
    • The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis
    • Bause, E., and G. Legler. 1981. The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis. Biochem. J. 195:639-644.
    • (1981) Biochem. J , vol.195 , pp. 639-644
    • Bause, E.1    Legler, G.2
  • 6
    • 35448967957 scopus 로고    scopus 로고
    • Disease duration determines canine distemper virus neurovirulence
    • Bonami, F., P. A. Rudd, and V. von Messling. 2007. Disease duration determines canine distemper virus neurovirulence. J. Virol. 81:12066-12070.
    • (2007) J. Virol , vol.81 , pp. 12066-12070
    • Bonami, F.1    Rudd, P.A.2    von Messling, V.3
  • 8
    • 19944415289 scopus 로고    scopus 로고
    • Role of N-linked glycosylation of the Hendra virus fusion protein
    • Carter, J. R., C. T. Pager, S. D. Fowler, and R. E. Dutch. 2005. Role of N-linked glycosylation of the Hendra virus fusion protein. J. Virol. 79:7922-7925.
    • (2005) J. Virol , vol.79 , pp. 7922-7925
    • Carter, J.R.1    Pager, C.T.2    Fowler, S.D.3    Dutch, R.E.4
  • 9
    • 0033020645 scopus 로고    scopus 로고
    • Sequence analysis and expression of the attachment and fusion proteins of canine distemper virus wild-type strain A75/17
    • Cherpillod, P., K. Beck, A. Zurbriggen, and R. Wittek. 1999. Sequence analysis and expression of the attachment and fusion proteins of canine distemper virus wild-type strain A75/17. J. Virol. 73:2263-2269.
    • (1999) J. Virol , vol.73 , pp. 2263-2269
    • Cherpillod, P.1    Beck, K.2    Zurbriggen, A.3    Wittek, R.4
  • 11
    • 0016740806 scopus 로고
    • Biological properties of a canine distemper virus isolate associated with demyelinating encephalomyelitis
    • Confer, A. W., D. E. Kahn, A. Koestner, and S. Krakowka. 1975. Biological properties of a canine distemper virus isolate associated with demyelinating encephalomyelitis. Infect. Immun. 11:835-844.
    • (1975) Infect. Immun , vol.11 , pp. 835-844
    • Confer, A.W.1    Kahn, D.E.2    Koestner, A.3    Krakowka, S.4
  • 12
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of Influenza virus hemagglutinin
    • Daniels, R., B. Kurowski, A. E. Johnson, and D. N. Hebert. 2003. N-linked glycans direct the cotranslational folding pathway of Influenza virus hemagglutinin. Mol. Cell 11:79-90.
    • (2003) Mol. Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 13
    • 35448970026 scopus 로고    scopus 로고
    • Measles virus
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus ed, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Griffin, D. E. 2006. Measles virus, p. 1551-1586. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2006) Fields virology , pp. 1551-1586
    • Griffin, D.E.1
  • 14
    • 0030928288 scopus 로고    scopus 로고
    • Analysis of the haemagglutinin gene of current wild-type canine distemper virus isolates from Germany
    • Haas, L., W. Martens, I. Greiser-Wilke, L. Mamaev, T. Butina, D. Maack, and T. Barrett. 1997. Analysis of the haemagglutinin gene of current wild-type canine distemper virus isolates from Germany. Virus Res. 48:165-171.
    • (1997) Virus Res , vol.48 , pp. 165-171
    • Haas, L.1    Martens, W.2    Greiser-Wilke, I.3    Mamaev, L.4    Butina, T.5    Maack, D.6    Barrett, T.7
  • 15
    • 0035915993 scopus 로고    scopus 로고
    • CDw150(SLAM) is a receptor for a lymphotropic strain of measles virus and may account for the immunosuppressive properties of this virus
    • Hsu, E. C., C. Iorio, F. Sarangi, A. A. Khine, and C. D. Richardson. 2001. CDw150(SLAM) is a receptor for a lymphotropic strain of measles virus and may account for the immunosuppressive properties of this virus. Virology 279:9-21.
    • (2001) Virology , vol.279 , pp. 9-21
    • Hsu, E.C.1    Iorio, C.2    Sarangi, F.3    Khine, A.A.4    Richardson, C.D.5
  • 16
    • 0028899494 scopus 로고
    • Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein
    • Hu, A., T. Cathomen, R. Cattaneo, and E. Norrby. 1995. Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein. J. Gen. Virol. 76:705-710.
    • (1995) J. Gen. Virol , vol.76 , pp. 705-710
    • Hu, A.1    Cathomen, T.2    Cattaneo, R.3    Norrby, E.4
  • 17
    • 0028256486 scopus 로고
    • Role of N-linked oligosaccharide chains in the processing and antigenicity of measles virus haemagglutinin protein
    • Hu, A., R. Cattaneo, S. Schwartz, and E. Norrby. 1994. Role of N-linked oligosaccharide chains in the processing and antigenicity of measles virus haemagglutinin protein. J. Gen. Virol. 75:1043-1052.
    • (1994) J. Gen. Virol , vol.75 , pp. 1043-1052
    • Hu, A.1    Cattaneo, R.2    Schwartz, S.3    Norrby, E.4
  • 18
    • 1642359898 scopus 로고    scopus 로고
    • Characterization of a region involved in binding of measles virus H protein and its receptor SLAM (CD150)
    • Hu, C., P. Zhang, X. Liu, Y. Qi, T. Zou, and Q. Xu. 2004. Characterization of a region involved in binding of measles virus H protein and its receptor SLAM (CD150). Biochem. Biophys. Res. Commun. 316:698-704.
    • (2004) Biochem. Biophys. Res. Commun , vol.316 , pp. 698-704
    • Hu, C.1    Zhang, P.2    Liu, X.3    Qi, Y.4    Zou, T.5    Xu, Q.6
  • 19
    • 0031020238 scopus 로고    scopus 로고
    • Molecular and phylogenetic analyses of the haemagglutinin (H) proteins of field isolates of canine distemper virus from naturally infected dogs
    • Iwatsuki, K., N. Miyashita, E. Yoshida, T. Gemma, Y.-S. Shin, T. Mori, N. Hirayama, C. Kai, and T. Mikami. 1997. Molecular and phylogenetic analyses of the haemagglutinin (H) proteins of field isolates of canine distemper virus from naturally infected dogs. J. Gen. Virol. 78:373-380.
    • (1997) J. Gen. Virol , vol.78 , pp. 373-380
    • Iwatsuki, K.1    Miyashita, N.2    Yoshida, E.3    Gemma, T.4    Shin, Y.-S.5    Mori, T.6    Hirayama, N.7    Kai, C.8    Mikami, T.9
  • 20
    • 0141458878 scopus 로고    scopus 로고
    • Assorted mutations in the envelope gene of simian immunodeficiency virus lead to loss of neutralization resistance against antibodies representing a broad spectrum of specificities
    • Johnson, W. E., H. Sanford, L. Schwall, D. R. Burton, P. W. H. I. Parren, J. E. Robinson, and R. C. Desrosiers. 2003. Assorted mutations in the envelope gene of simian immunodeficiency virus lead to loss of neutralization resistance against antibodies representing a broad spectrum of specificities. J. Virol. 77:9993-10003.
    • (2003) J. Virol , vol.77 , pp. 9993-10003
    • Johnson, W.E.1    Sanford, H.2    Schwall, L.3    Burton, D.R.4    Parren, P.W.H.I.5    Robinson, J.E.6    Desrosiers, R.C.7
  • 21
    • 0344665682 scopus 로고    scopus 로고
    • Recombinant measles AIK-C strain expressing current wild-type hemagglutinin protein
    • Kumada, A., K. Komase, and T. Nakayama. 2004. Recombinant measles AIK-C strain expressing current wild-type hemagglutinin protein. Vaccine 22:309-316.
    • (2004) Vaccine , vol.22 , pp. 309-316
    • Kumada, A.1    Komase, K.2    Nakayama, T.3
  • 22
    • 0030806423 scopus 로고    scopus 로고
    • Sequence and structure alignment of Paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin
    • Langedijk, J. P. M., F. J. Daus, and J. T. van Oirschot. 1997. Sequence and structure alignment of Paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin. J. Virol. 71:6155-6167.
    • (1997) J. Virol , vol.71 , pp. 6155-6167
    • Langedijk, J.P.M.1    Daus, F.J.2    van Oirschot, J.T.3
  • 23
    • 47749143663 scopus 로고    scopus 로고
    • Functional interaction between paramyxovirus fusion and attachment proteins
    • Lee, J. K., A. Prussia, T. Paal, L. K. White, J. P. Snyder, and R. K. Plemper. 2008. Functional interaction between paramyxovirus fusion and attachment proteins. J. Biol. Chem. 283:16561-16572.
    • (2008) J. Biol. Chem , vol.283 , pp. 16561-16572
    • Lee, J.K.1    Prussia, A.2    Paal, T.3    White, L.K.4    Snyder, J.P.5    Plemper, R.K.6
  • 24
    • 33744931897 scopus 로고    scopus 로고
    • RNA polymerase II-controlled expression of antigenomic RNA enhances the rescue efficacies of two different members of the Mononegavirales independently of the site of viral genome replication
    • Martin, A., P. Staeheli, and U. Schneider. 2006. RNA polymerase II-controlled expression of antigenomic RNA enhances the rescue efficacies of two different members of the Mononegavirales independently of the site of viral genome replication. J. Virol. 80:5708-5715.
    • (2006) J. Virol , vol.80 , pp. 5708-5715
    • Martin, A.1    Staeheli, P.2    Schneider, U.3
  • 25
    • 4143051366 scopus 로고    scopus 로고
    • Measles virus (MV) hemagglutinin: Evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head
    • Massé, N., M. Ainouze, B. Néel, T. F. Wild, R. Buckland, and J. P. M. Langedijk. 2004. Measles virus (MV) hemagglutinin: evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head. J. Virol. 78:9051-9063.
    • (2004) J. Virol , vol.78 , pp. 9051-9063
    • Massé, N.1    Ainouze, M.2    Néel, B.3    Wild, T.F.4    Buckland, R.5    Langedijk, J.P.M.6
  • 26
    • 0035837043 scopus 로고    scopus 로고
    • Carbohydrate modifications of the NDV fusion protein heptad repeat domains influence maturation and fusion activity
    • McGinnes, L., T. Sergel, J. Reittner, and T. Morrison. 2001. Carbohydrate modifications of the NDV fusion protein heptad repeat domains influence maturation and fusion activity. Virology 283:332-342.
    • (2001) Virology , vol.283 , pp. 332-342
    • McGinnes, L.1    Sergel, T.2    Reittner, J.3    Morrison, T.4
  • 27
    • 0028858321 scopus 로고
    • The role of individual oligosaccharide chains in the activities of the HN glycoprotein of Newcastle disease virus
    • McGinnes, L. W., and T. G. Morrison. 1995. The role of individual oligosaccharide chains in the activities of the HN glycoprotein of Newcastle disease virus. Virology 212:398-410.
    • (1995) Virology , vol.212 , pp. 398-410
    • McGinnes, L.W.1    Morrison, T.G.2
  • 28
    • 0025297484 scopus 로고    scopus 로고
    • Miletich, J. P., and G. J. Broze, Jr. 1990. β Protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites. J. Biol. Chem. 265:11397-11404.
    • Miletich, J. P., and G. J. Broze, Jr. 1990. β Protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites. J. Biol. Chem. 265:11397-11404.
  • 29
    • 0032773413 scopus 로고    scopus 로고
    • Genotypes of canine distemper virus determined by analysis of the hemagglutinin genes of recent isolates from dogs in Japan
    • Mochizuki, M., M. Hashimoto, S. Hagiwara, Y. Yoshida, and S, Ishiguro. 1999. Genotypes of canine distemper virus determined by analysis of the hemagglutinin genes of recent isolates from dogs in Japan. J. Clin. Microbiol. 37:2936-2942.
    • (1999) J. Clin. Microbiol , vol.37 , pp. 2936-2942
    • Mochizuki, M.1    Hashimoto, M.2    Hagiwara, S.3    Yoshida, Y.4    Ishiguro, S.5
  • 30
    • 2942647917 scopus 로고    scopus 로고
    • Influence of N-glycans on processing and biological activity of the Nipah virus fusion protein
    • Moll, M., A. Kaufmann, and A. Maisner. 2004. Influence of N-glycans on processing and biological activity of the Nipah virus fusion protein. J. Virol. 78:7274-7278.
    • (2004) J. Virol , vol.78 , pp. 7274-7278
    • Moll, M.1    Kaufmann, A.2    Maisner, A.3
  • 31
    • 0025342516 scopus 로고
    • Different roles of individual N-linked oligosaccharide chains in folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase
    • Ng, D. T. W., S. W. Hiebert, and R. A. Lamb. 1990. Different roles of individual N-linked oligosaccharide chains in folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase. Mol. Cell. Biol. 10:1989-2001.
    • (1990) Mol. Cell. Biol , vol.10 , pp. 1989-2001
    • Ng, D.T.W.1    Hiebert, S.W.2    Lamb, R.A.3
  • 32
    • 36049013168 scopus 로고    scopus 로고
    • Localization and membrane topology of coronavirus nonstructural protein 4: Involvement of the early secretory pathway in replication
    • Oostra, M., E. G. te Lintelo, M. Deijs, M. H. Verheije, P. J. M. Rottier, and C. A. M. de Haan. 2007. Localization and membrane topology of coronavirus nonstructural protein 4: involvement of the early secretory pathway in replication. J. Virol. 81:12323-12336.
    • (2007) J. Virol , vol.81 , pp. 12323-12336
    • Oostra, M.1    te Lintelo, E.G.2    Deijs, M.3    Verheije, M.H.4    Rottier, P.J.M.5    de Haan, C.A.M.6
  • 33
    • 0037213889 scopus 로고    scopus 로고
    • Extent of measles virus spread and immune suppression differentiates between wild-type and vaccine strains in the cotton rat model (Sigmodon hispidus)
    • Pfeuffer, J., K. Puschel, V. ter Meulen, J. Schneider-Schaulies, and S. Niewiesk. 2003. Extent of measles virus spread and immune suppression differentiates between wild-type and vaccine strains in the cotton rat model (Sigmodon hispidus). J. Virol. 77:150-158.
    • (2003) J. Virol , vol.77 , pp. 150-158
    • Pfeuffer, J.1    Puschel, K.2    ter Meulen, V.3    Schneider-Schaulies, J.4    Niewiesk, S.5
  • 34
    • 0031749469 scopus 로고    scopus 로고
    • A role for carbohydrates in immune evasion in AIDS
    • Reitter, J. N., R. E. Means, and R. C. Desrosiers. 1998. A role for carbohydrates in immune evasion in AIDS. Nat. Med. 4:679-684.
    • (1998) Nat. Med , vol.4 , pp. 679-684
    • Reitter, J.N.1    Means, R.E.2    Desrosiers, R.C.3
  • 35
    • 0028197143 scopus 로고
    • Comparison of sequences of the H, F, and N coding genes of measles virus vaccine strains
    • Rota, J. S., Z.-D. Wang, P. A. Rota, and W. J. Bellini. 1994. Comparison of sequences of the H, F, and N coding genes of measles virus vaccine strains. Virus Res. 31:317-330.
    • (1994) Virus Res , vol.31 , pp. 317-330
    • Rota, J.S.1    Wang, Z.-D.2    Rota, P.A.3    Bellini, W.J.4
  • 36
    • 67650588773 scopus 로고    scopus 로고
    • A chimeric measles virus with canine distemper envelope protects ferrets from lethal distemper challenge
    • Rouxel, R. N., N. Svitek, and V. von Messling. 2009. A chimeric measles virus with canine distemper envelope protects ferrets from lethal distemper challenge. Vaccine 27:4961-4966.
    • (2009) Vaccine , vol.27 , pp. 4961-4966
    • Rouxel, R.N.1    Svitek, N.2    von Messling, V.3
  • 37
    • 33846813688 scopus 로고    scopus 로고
    • Inhibition of henipavirus infection by Nipah virus attachment glycoprotein occurs without cell surface down-regulation of ephrin-B2 or ephrin-B3
    • Sawatsky, B., A. Grolla, N. Kuzenko, H. Weingartl, and M. Czub. 2007. Inhibition of henipavirus infection by Nipah virus attachment glycoprotein occurs without cell surface down-regulation of ephrin-B2 or ephrin-B3. J. Gen. Virol. 88:582-591.
    • (2007) J. Gen. Virol , vol.88 , pp. 582-591
    • Sawatsky, B.1    Grolla, A.2    Kuzenko, N.3    Weingartl, H.4    Czub, M.5
  • 39
    • 0042924245 scopus 로고    scopus 로고
    • Functional analysis of individual oligosaccharide chains of Sendai virus hemagglutinin-neuraminidase protein
    • Segawa, H., A. Inakawa, T. Yamashita, and H. Taira. 2003. Functional analysis of individual oligosaccharide chains of Sendai virus hemagglutinin-neuraminidase protein. Biosci. Biotechnol. Biochem. 67:592-598.
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 592-598
    • Segawa, H.1    Inakawa, A.2    Yamashita, T.3    Taira, H.4
  • 40
    • 0033914327 scopus 로고    scopus 로고
    • Functional analysis of the individual oligosaccharide chains of Sendai virus fusion protein
    • Segawa, H., T. Yamashita, M. Kawakita, and H. Taira. 2000. Functional analysis of the individual oligosaccharide chains of Sendai virus fusion protein. J. Biochem. 128:65-72.
    • (2000) J. Biochem , vol.128 , pp. 65-72
    • Segawa, H.1    Yamashita, T.2    Kawakita, M.3    Taira, H.4
  • 41
    • 0020491258 scopus 로고
    • Amino acid sequence of the heavy chain of bovine protein
    • Stenflo, J., and P. Fernlund. 1982. Amino acid sequence of the heavy chain of bovine protein C. J. Biol. Chem. 257:12180-12190.
    • (1982) C. J. Biol. Chem , vol.257 , pp. 12180-12190
    • Stenflo, J.1    Fernlund, P.2
  • 42
    • 0034710650 scopus 로고    scopus 로고
    • SLAM (CDw150) is a cellular receptor for measles virus
    • Tatsuo, H., N. Ono, K. Tanaka, and Y. Yanagi. 2000. SLAM (CDw150) is a cellular receptor for measles virus. Nature 406:893-897.
    • (2000) Nature , vol.406 , pp. 893-897
    • Tatsuo, H.1    Ono, N.2    Tanaka, K.3    Yanagi, Y.4
  • 45
    • 0030866216 scopus 로고    scopus 로고
    • Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and atypical (Asn-X-Cys) glycosylation motifs
    • Vance, B. A., W. Wu, R. K. Ribaudo, D. M. Segal, and K. P. Kearse. 1997. Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and atypical (Asn-X-Cys) glycosylation motifs. J. Biol. Chem. 272:23117-23122.
    • (1997) J. Biol. Chem , vol.272 , pp. 23117-23122
    • Vance, B.A.1    Wu, W.2    Ribaudo, R.K.3    Segal, D.M.4    Kearse, K.P.5
  • 46
    • 0345734198 scopus 로고    scopus 로고
    • Selectively receptor-blind measles viruses: Identification of residues necessary for SLAM- or CD46-induced fusion and their localization on a new hemagglutinin structural model
    • Vongpunsawad, S., N. Oezgun, W. Braun, and R. Cattaneo. 2004. Selectively receptor-blind measles viruses: identification of residues necessary for SLAM- or CD46-induced fusion and their localization on a new hemagglutinin structural model. J. Virol. 78:302-313.
    • (2004) J. Virol , vol.78 , pp. 302-313
    • Vongpunsawad, S.1    Oezgun, N.2    Braun, W.3    Cattaneo, R.4
  • 47
    • 0141521694 scopus 로고    scopus 로고
    • N-linked glycans with similar location in the fusion protein head modulate paramyxovirus fusion
    • von Messling, V., and R. Cattaneo. 2003. N-linked glycans with similar location in the fusion protein head modulate paramyxovirus fusion. J. Virol. 77:10202-10212.
    • (2003) J. Virol , vol.77 , pp. 10202-10212
    • von Messling, V.1    Cattaneo, R.2
  • 48
    • 4644291832 scopus 로고    scopus 로고
    • Tropism illuminated: Lymphocyte-based pathways blazed by lethal morbillivirus through the host immune system
    • von Messling, V., D. Milosevic, and R. Cattaneo. 2004. Tropism illuminated: lymphocyte-based pathways blazed by lethal morbillivirus through the host immune system. Proc. Natl. Acad. Sci. U. S. A. 101:14216-14221.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 14216-14221
    • von Messling, V.1    Milosevic, D.2    Cattaneo, R.3
  • 49
    • 17444379724 scopus 로고    scopus 로고
    • Nearby clusters of hemagglutinin residues sustain SLAM-dependent canine distemper virus entry in peripheral blood mononuclear cells
    • von Messling, V., N. Oezguen, Q. Zheng, S. Vongpunsawad, W. Braun, and R. Cattaneo. 2005. Nearby clusters of hemagglutinin residues sustain SLAM-dependent canine distemper virus entry in peripheral blood mononuclear cells. J. Virol. 79:5857-5862.
    • (2005) J. Virol , vol.79 , pp. 5857-5862
    • von Messling, V.1    Oezguen, N.2    Zheng, Q.3    Vongpunsawad, S.4    Braun, W.5    Cattaneo, R.6
  • 50
    • 0242409386 scopus 로고    scopus 로고
    • A ferret model of canine distemper virus virulence and immunosuppression
    • von Messling, V., C. Springfeld, P. Devaux, and R. Cattaneo. 2003. A ferret model of canine distemper virus virulence and immunosuppression. J. Virol. 77:12579-12591.
    • (2003) J. Virol , vol.77 , pp. 12579-12591
    • von Messling, V.1    Springfeld, C.2    Devaux, P.3    Cattaneo, R.4
  • 51
    • 33744899576 scopus 로고    scopus 로고
    • Receptor (SLAM [CD150]) recognition and the V protein sustain swift lymphocyte-based invasion of mucosal tissue and lymphatic organs by a morbillivirus
    • von Messling, V., N. Svitek, and R. Cattaneo. 2006. Receptor (SLAM [CD150]) recognition and the V protein sustain swift lymphocyte-based invasion of mucosal tissue and lymphatic organs by a morbillivirus. J. Virol. 80:6084-6092.
    • (2006) J. Virol , vol.80 , pp. 6084-6092
    • von Messling, V.1    Svitek, N.2    Cattaneo, R.3
  • 52
    • 0034979292 scopus 로고    scopus 로고
    • The hemagglutinin of canine distemper virus determines tropism and cytopathogenicity
    • von Messling, V., G. Zimmer, G. Herrler, L. Haas, and R. Cattaneo. 2001. The hemagglutinin of canine distemper virus determines tropism and cytopathogenicity. J. Virol. 75:6418-6427.
    • (2001) J. Virol , vol.75 , pp. 6418-6427
    • von Messling, V.1    Zimmer, G.2    Herrler, G.3    Haas, L.4    Cattaneo, R.5
  • 54
    • 0033864317 scopus 로고    scopus 로고
    • Measles virus-induced immunosuppression in vitro is independent of complex glycosylation of viral glycoproteins and of hemifusion
    • Weidmann, A., C. Fischer, S. Ohgimoto, C. Rüth, V. ter Meulen, and S. Schneider-Schaulies. 2000. Measles virus-induced immunosuppression in vitro is independent of complex glycosylation of viral glycoproteins and of hemifusion. J. Virol. 74:7548-7553.
    • (2000) J. Virol , vol.74 , pp. 7548-7553
    • Weidmann, A.1    Fischer, C.2    Ohgimoto, S.3    Rüth, C.4    ter Meulen, V.5    Schneider-Schaulies, S.6
  • 55
    • 0033934369 scopus 로고    scopus 로고
    • Proteolytic cleavage of the fusion protein but not membrane fusion is required for measles virus-induced immunosuppression in vitro
    • Weidmann, A., A. Maisner, W. Garten, M. Seufert, V. ter Meulen, and S. Schneider-Schaulies. 2000. Proteolytic cleavage of the fusion protein but not membrane fusion is required for measles virus-induced immunosuppression in vitro. J. Virol. 74:1985-1993.
    • (2000) J. Virol , vol.74 , pp. 1985-1993
    • Weidmann, A.1    Maisner, A.2    Garten, W.3    Seufert, M.4    ter Meulen, V.5    Schneider-Schaulies, S.6


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