Membrane-anchored incorporation of a foreign protein in recombinant influenza virions

Virology

Volumn 246, Issue 1, 1998, Pages 83-94

  Zhou, Yan ^a   König, Matthias ^a   Hobom, Gerd ^a   Neumeier, Elisabeth ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; DNA DIRECTED RNA POLYMERASE; HN PROTEIN; HYBRID PROTEIN; VIRUS GLYCOPROTEIN; VIRUS RNA;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; INFLUENZA VIRUS; INFLUENZA VIRUS A; KIDNEY CELL; NONHUMAN; PESTIVIRUS; PRIORITY JOURNAL; VIRION; VIRUS ENVELOPE; VIRUS PARTICLE; VIRUS RECOMBINANT;

ANIMALIA; CLASSICAL SWINE FEVER VIRUS; INFLUENZA VIRUS; INFLUENZAVIRUS A; PESTIVIRUS; RNA VIRUSES; SUS SCROFA;

EID: 0032551238     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9169     Document Type: Article

References (46)

1. Castrucci, M. R., Bilsel, P., and Kawaoka, Y. (1992). Attenuation of influenza A virus by insertion of a foreign epitope into the neuraminidase. J. Virol. 66, 4647-4653.
2. Chalfie, M., Tu, Y., Euskirchen, G., Ward, W. W., Prasher, D. C. (1994). Green fluorescent protein as a marker for gene expression. Science 263, 802-805.
3. Collier, N. C., Knox, K., and Schlesinger, M. J. (1991). Inhibition of influenza virus formation by a peptide that corresponds to sequences in the cytoplasmic domain of the hemagglutinin. Virology 183, 769-772.
4. Doyle, C., Roth, M. G., Sambrook, J., and Gething, M. J. (1985). Mutations in the cytoplasmic domain of the influenza virus hemagglutinin affect different stages of intracellular transport. J. Cell. Biol. 100, 704-714.
5. Enami, M., and Enami, K. (1996). Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein. J. Virol. 70(10) 6653-6657.
6. Enami, M., Sharma, G., Benham, C., and Palese, P. (1991). An influenza virus containing nine different RNA segments. Virology 185, 291-298.
7. Fiedler, K., Veit, M., Stamnes, M. A., and Rothman, J. E. (1996). Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science 273, 1396-1398.
8. Flick, R., Neumann, G., Hoffmann, E., Neumeier, E., and Hobom, G. (1996). Promoter elements in the influenza vRNA terminal structure. RNA 2, 1046-1057.
9. Gaedigk-Nitschko, K., and Schlesinger, M. J. (1991). Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding. Virology 183, 206-214.
10. García-Sastre, A., and Palese, P. (1995). The cytoplasmic tail of the neuraminidase protein of influenza A virus does not play an important role in the packaging of this protein into viral envelopes. Virus Res. 37, 37-47.
11. Garcia-Sastre, A., Muster, T., Barclay, W. S., Percy, N., and Palese, P. (1994). Use of a mammalian internal ribosomal entry site element for expression of a foreign protein by a transfectant influenza virus. J. Virol. 68(10), 6254-6261.
12. Jin, H., Leser, G. P., and Lamb, R. A. (1994). The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity. EMBO J. 13, 5504-5515.
13. Jin, H., Subbarao, K., Bagai, S., Leser, G. P., Murphy, B. R., and Lamb, R. A. (1996). Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity. J. Virol. 70(3), 1406-1414.
14. König, M., Lengsfeld, T., Pauly, T., Stark, R., and Thiel, H.-J. (1995). Classical swine fever virus: Independent induction of protective immunity by two structural glycoproteins. J. Virol. 69(10), 6479-6486.
15. Kozak, M. (1989). The scanning model for translation: An update. J. Cell. Biol. 108, 229-241.
16. Kretzschmar, E., Buonocore, L., Schnell, M. J., and Rose, J. K. (1997). High-efficiency incorporation of functional influenza virus glycoproteins into recombinant vesicular stomatitis virus. J. Virol. 71, 5982-5989.
17. Lamb, R. A., and Krug, R. M. (1996) Orthomyxoviridae: The viruses and their replication. In 'Virology' (B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus, Eds.), 3rd ed., Vol. 1, pp. 1353-1395. Lippincott-Raven, Philadelphia.
18. Li, S., Schulman, J. L., Moran, T., Bona, C., and Palese, P. (1992). Influenza A virus transfectants with chimeric hemagglutinins containing epitopes from different subtypes. J. Virol. 66, 399-404.
19. Li, S., Rodrigues, M., Rodriguez, D., Rodriguez, J. R., Esteban, M., Palese, P., Nussenzweig, R. S., and Zavala, F. (1993). Priming with recombinant influenza virus followed by administration of recombinant vaccinia virus induces CD8+ T-cell-mediated protective immunity against malaria. Proc. Natl. Acad. Sci. USA 90, 5214-5218.
20. Luytjes, W., Krystal, M., Enami, M., Parvin, J. D., and Palese, P. (1989). Amplification, expression, and packaging of a foreign gene by influenza virus. Cell 59, 1107-1113.
21. McDougall, J. K., Masse, T. H., and Galloway, D. A. (1980). Location and cloning of the herpes simplex virus type 2 thymidine kinase gene. J. Virol. 33, 1221-1224.
22. Mena, I., Vivo, A., Perez, E., and Portela, A. (1996). Rescue of a synthetic chloramphenicol acetyltransferase RNA into influenza virus-like particles obtained from recombinant plasmids. J. Virol. 70, 5016-5024.
23. Meyers, G., Rümenapf, T., and Thiel, H.-J. (1989). Molecular cloning and nucleotide sequence of the genome of Hog Cholera Virus. Virology 171, 555-567.
24. Mitnaul, L. J., Castrucci, M. R., Murti, K. G., and Kawaoka, Y. (1996). The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication. J. Virol. 70(2), 873-879.
25. Muster, T., Guinea, R., Trkola, A., Purtscher, M., Klima, A., Steindl, F., Palese, P., and Katinger, H. (1994). Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. J. Virol. 68, 4031-4034.
26. Muster, T., Ferko, B., Klima, A., Purtscher, M., Trkola, A., Schulz, P., Grassauer, A., Engelhardt, O. G., García-Sastre, A., Palese, P. et al. (1995). Mucosal model of immunization against human immunodeficiency virus type 1 with a chimeric influenza virus. J. Virol. 69(11), 6678-6686.
27. Naeve, C. W., and Williams, D. (1990). Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion. EMBO J. 9, 3857-3866.
28. Naim, H. Y., and Roth, M. G. (1993). Basis for selective incorporation of glycoproteins into the influenza virus envelope. J. Virol. 67(8), 4831-4841.
29. Neumann, G., and Hobom, G. (1995). Mutational analysis of influenza virus promoter elements in vivo. J. Gen. Virol. 76, 1709-1717.
30. Neumann, G., Zobel, A., and Hobom, G. (1994). RNA polymerase I-mediated expression of influenza viral RNA molecules. Virology 202, 477-479.
31. Nishimura, N., and Balch, W. E. (1997). A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277, 556-558.
32. Nobusawa, E., Aoyama, T., Kato, H., Suzuki, Y., Tateno, Y., and Nakajima, K. (1991). Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 182, 475-485.
33. Percy, N., Barclay, W. S., Garcia-Sastre, A., and Palese, P. (1994). Expression of a foreign protein by influenza A virus. J. Virol. 68(7), 4486-4492.
34. Rice, C. M. (1996) Flaviviridae: The viruses and their replication. In 'Virology' (B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus, Eds.), 3rd ed., Vol. 1, pp. 1059-1073. Lippincott-Raven, Philadelphia.
35. Siemering, K. R., Golbik, R., Sever, R., and Haseloff, J. (1996). Mutations that suppress the thermosensitivity of green fluorescent protein. Curr. Biol. 6, 1653-1663.
36. Stark, R., Meyers, G., Rumenapf, T., and Thiel, H. J. (1993). Processing of pestivirus polyprotein: Cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus. J. Virol. 67(12), 7088-7095.
37. Thiel, H.-J., Plagemann, P. G. W., and Moennig, V. (1996). Pestiviruses. In 'Virology' (B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus, Eds.), 3rd ed., Vol. 1, pp. 1059-1073. Lippincott-Raven, Philadelphia.
38. Thomas, D. C., and Roth, M. G. (1994). The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from Vesicular Stomatitis Virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities. J. Biol. Chem. 169, 15732-15739.
39. Veit, M., Kretzschmar, E., Kuroda, K., Garten, W., Schmidt, M. F. G., Klenk, H.-D., and Rott, R. (1991). Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin. J. Virol. 65(5), 2491-2500.
40. Weiland, E., Stark, R., Haas, B., Rumenapf, T., Meyers, G., and Thiel, H. J. (1990). Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer. J. Virol. 64(8), 3563-3569.
41. Weiland, E., Ahl, R., Stark, R., Weiland, F., and Thiel, H.-J. (1992). A second envelope glycoprotein mediates neutralization of a pestivirus, hog cholera virus. J. Virol. 66, 3677-3682.
42. Whitt, M. A., Chong, L., and Rose, J. K. (1989). Glycoprotein cytoplasmic domain sequences required for rescue of a Vesicular Stomatitis Virus glycoprotein mutant. J. Virol. 63, 3569-3578.
43. Yao, Q., and Compans, R. W. (1995). Differences in the role of the cytoplasmic domain of human parainfluenza virus fusion proteins. J. Virol. 69(11), 7045-7053.
44. Zebedee, S. L., and Lamb, R. A. (1988). Influenza A virus M2 protein: Monoclonal antibody restriction of virus growth and detection of M2 in virions. J. Virol. 62(8), 2762-2772.
45. Zobel, A., Neumann, G., and Hobom, G. (1993). RNA polymerase I catalysed transcription of insert viral cDNA. Nucleic Acids Res. 21, 3607-3614.
46. Zurcher, T., Luo, G., and Palese, P. (1994). Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation. J. Virol. 68(9), 5748-5754.