Addition of a single N-glycan to street rabies virus glycoprotein enhances virus production

Journal of General Virology

Volumn 94, Issue PART2, 2013, Pages 270-275

  Yamada, Kentaro ^a   Noguchi, Kazuko ^a,b   Nonaka, Daichi ^b   Morita, Muneshin ^b   Yasuda, Aiko ^a   Kawazato, Hiroaki ^a   Nishizono, Akira ^a,b  

^a OITA UNIVERSITY   (Japan)

^b OITA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; GLYCAN; GLYCOPROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN;

ARTICLE; CONTROLLED STUDY; GENE DELETION; GLYCOSYLATION; NERVE CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STRUCTURE; RABIES VIRUS;

ANTIGENS, VIRAL; CELL LINE; GLYCOPROTEINS; GLYCOSYLATION; POLYSACCHARIDES; RABIES VIRUS; VIRAL ENVELOPE PROTEINS; VIRULENCE FACTORS; VIRUS REPLICATION;

RABIES VIRUS;

EID: 84872432947     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.047852-0     Document Type: Article

References (19)

1. Badrane, H. & Tordo, N. (2001). Host switching in Lyssavirus history from the Chiroptera to the Carnivora orders. J Virol 75, 8096-8104.
2. Gaudin, Y. (1997). Folding of rabies virus glycoprotein: epitope acquisition and interaction with endoplasmic reticulum chaperones. J Virol 71, 3742-3750.
3. Hiramatsu, K., Mifune, K., Mannen, K., Nishizono, A., Kawano, H., Ito, Y. & Kawai, A. (1992). Mapping of the antigenic determinants recognized by monoclonal antibodies against the M2 protein of rabies virus. Virology 187, 472-479.
4. Irie, T., Matsuda, Y., Honda, Y., Morimoto, K. & Kawai, A. (2002). Studies on the escape mutants of rabies virus which are resistant to neutralization by a highly conserved conformational epitope-specific monoclonal antibody #1-46-12. Microbiol Immunol 46, 449-461.
5. Ito, N., Takayama, M., Yamada, K., Sugiyama, M. & Minamoto, N. (2001). Rescue of rabies virus from cloned cDNA and identification of the pathogenicity-related gene: glycoprotein gene is associated with virulence for adult mice. J Virol 75, 9121-9128.
6. Ito, N., Takayama-Ito, M., Yamada, K., Hosokawa, J., Sugiyama, M. & Minamoto, N. (2003). Improved recovery of rabies virus from cloned cDNA using a vaccinia virus-free reverse genetics system. Microbiol Immunol 47, 613-617.
7. Ito, K., Ishimaru, T., Kimura, F. & Matsudomi, N. (2007a). Importance of N-glycosylation positioning for secretion and folding of ovalbumin. Biochem Biophys Res Commun 361, 725-731.
8. Ito, K., Seri, A., Kimura, F. & Matsudomi, N. (2007b). Site-specific glycosylation at Asn-292 in ovalbumin is essential to efficient secretion in yeast. J Biochem 141, 193-199.
9. Kasturi, L., Eshleman, J. R., Wunner, W. H. & Shakin-Eshleman, S. H. (1995). The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein. J Biol Chem 270, 14756-14761.
10. Kayser, V., Chennamsetty, N., Voynov, V., Forrer, K., Helk, B. & Trout, B. L. (2011). Glycosylation influences on the aggregation propensity of therapeutic monoclonal antibodies. Biotechnol J 6, 38-44.
11. Luo, T. R., Minamoto, N., Ito, H., Goto, H., Hiraga, S., Ito, N., Sugiyama, M. & Kinjo, T. (1997). A virus-neutralizing epitope on the glycoprotein of rabies virus that contains Trp251 is a linear epitope. Virus Res 51, 35-41.
12. Shakin-Eshleman, S. H., Remaley, A. T., Eshleman, J. R., Wunner, W. H. & Spitalnik, S. L. (1992). N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression. J Biol Chem 267, 10690-10698.
13. Shakin-Eshleman, S. H., Spitalnik, S. L. & Kasturi, L. (1996). The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency. J Biol Chem 271, 6363-6366.
14. Shiota, S., Mannen, K., Matsumoto, T., Yamada, K., Yasui, T., Takayama, K., Kobayashi, Y., Khawplod, P., Gotoh, K. & other authors (2009). Development and evaluation of a rapid neutralizing antibody test for rabies. J Virol Methods 161, 58-62.
15. Somnuke, P., Hauhart, R. E., Atkinson, J. P., Diamond, M. S. & Avirutnan, P. (2011). N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement. Virology 413, 253-264.
16. Wunner, W. H. (2007). Rabies virus. In Rabies, 2nd edn, pp. 23-68. Edited by A. C. Jackson & W. H. Wunner. San Diego, CA: Academic Press.
17. Wunner, W. H., Dietzschold, B., Smith, C. L., Lafon, M. & Golub, E. (1985). Antigenic variants of CVS rabies virus with altered glycosylation sites. Virology 140, 1-12.
18. Yamada, K., Park, C. H., Noguchi, K., Kojima, D., Kubo, T., Komiya, N.,Matsumoto, T., Mitui, M. T., Ahmed, K. & other authors (2012). Serial passage of a street rabies virus in mouse neuroblastoma cells resulted in attenuation: potential role of the additional N-glycosylation of a viral glycoprotein in the reduced pathogenicity of street rabies virus. Virus Res 165, 34-45.
19. Zhou, W. & Tsai, H. M. (2009). N-Glycans of ADAMTS13 modulate its secretion and vonWillebrand factor cleaving activity. Blood 113, 929-935.