Abstract

Our long term goal is to elucidate the structure and genesis of defective interfering (DI) influenza virus, the mechanism of DI influenza virus mediated interference and hopefully, the role of the DI virus in the evolution and the diversity of influenza viruses in nature. In this present project our specific objectives are to further investigate the structure of DI RNA and its relationship to progenitor RNAs, to investigate the transcription and translation products of DI RNA in vitro and in infected cells, to establish an in vitro system of influenza viral RNA replication, and finally to determine the role of DI viruses viral persistency and diversity. DI virus from influenza A, B and C type viruses will be produced by passing virus at a high multiplicity using productive cell-virus systems. DI viruses will be amplifed using homologous standard virus as helper. Detailed structure analyses of DI RNA and their relationship to the progenitor genes will be performed by DNA cloning, heteroduplex mapping, restriction analyses and sequence determination. The mechanism of DI virus mediated interference will be elucidated by studying the transcription and replication of DI viral RNA in vitro as well as in infected cell. Subsequently, the effect of DI virus on the transcription and replication of standard viral RNAs will be determined both in vitro replication and transcription systems as well as in cells coinfected with both DI virus and standard virus. The role of DI viruses will be investigated by isolating variant viruses resistant DI mediated interference and determining the gene(s) responsible for the resistance.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI012749-11
Application #
3125277
Study Section
Virology Study Section (VR)
Project Start
1975-06-01
Project End
1988-11-30
Budget Start
1985-12-01
Budget End
1986-11-30
Support Year
11
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of California Los Angeles
Department
Type
Schools of Medicine
DUNS #
119132785
City
Los Angeles
State
CA
Country
United States
Zip Code
90095

  Publications

Biswas, S K; Nayak, D P (1996) Influenza virus polymerase basic protein 1 interacts with influenza virus polymerase basic protein 2 at multiple sites. J Virol 70:6716-22
Kundu, A; Nayak, D P (1994) Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins. J Virol 68:1812-8
Sanderson, C M; Wu, H H; Nayak, D P (1994) Sendai virus M protein binds independently to either the F or the HN glycoprotein in vivo. J Virol 68:69-76
Hogue, B G; Nayak, D P (1994) Deletion mutation in the signal anchor domain activates cleavage of the influenza virus neuraminidase, a type II transmembrane protein. J Gen Virol 75 ( Pt 5):1015-22
Biswas, S K; Nayak, D P (1994) Mutational analysis of the conserved motifs of influenza A virus polymerase basic protein 1. J Virol 68:1819-26
Gujuluva, C N; Kundu, A; Murti, K G et al. (1994) Abortive replication of influenza virus A/WSN/33 in HeLa229 cells: defective viral entry and budding processes. Virology 204:491-505
Sanderson, C M; McQueen, N L; Nayak, D P (1993) Sendai virus assembly: M protein binds to viral glycoproteins in transit through the secretory pathway. J Virol 67:651-63
Rey, O; Nayak, D P (1992) Nuclear retention of M1 protein in a temperature-sensitive mutant of influenza (A/WSN/33) virus does not affect nuclear export of viral ribonucleoproteins. J Virol 66:5815-24
Hogue, B G; Nayak, D P (1992) Synthesis and processing of the influenza virus neuraminidase, a type II transmembrane glycoprotein. Virology 188:510-7
Kundu, A; Jabbar, M A; Nayak, D P (1991) Cell surface transport, oligomerization, and endocytosis of chimeric type II glycoproteins: role of cytoplasmic and anchor domains. Mol Cell Biol 11:2675-85

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