Functional defects of fowl plague virus temperature-sensitive mutant having mutation in the neuraminidase
- 1 March 1983
- journal article
- research article
- Published by Springer Nature in Archiv für die gesamte Virusforschung
- Vol. 75 (1-2) , 55-70
- https://doi.org/10.1007/bf01314127
Abstract
A fowl plague virus (FPV) temperature-sensitive mutantts 5 having mutation lesions in the gene coding for the neuraminidase has been obtained. The mutant induced synthesis of cRNA, vRNA and proteins in cells under non-permissive conditions, but formation of virions including non-infectious ones was defective. The neuraminidase and haemagglutinin synthesized under non-permissive conditions possessed functional activity and could migrate from the rough endoplasmic reticulum into plasma membranes; however, cleavage of the haem-agglutinin was reduced. Ints 5-infected cells under non-permissive conditions the synthesis of segments 5 and 8 of cRNA and vRNA was predominant both early and late in the reproduction cycle, and the synthesis of P1, P2, P3, HA and M proteins was reduced after approximately 3 hours. The data obtained suggest that involvement of the neuraminidase in the formation of infectious virions may have no direct association with the enzymatic activity of this protein, and that the mutation in the neuraminidase may affect regulation of replication and transcription processes.Keywords
This publication has 32 references indexed in Scilit:
- Ultrastructural Changes in Cells Induced by Temperature-sensitive Mutants of Fowl Plague Virus at Permissive and Non-permissive TemperatureJournal of General Virology, 1980
- Genetics - Studies on mutation lesions and physiology of fowl plague virus ts mutantsPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1980
- Replication of Two Influenza Virus Strains and a Recombinant in HEF and LEP CellsJournal of General Virology, 1979
- Investigation of Recombinants of Human Influenza and Fowl Plague VirusesJournal of General Virology, 1979
- Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptideVirology, 1975
- Activation of influenza A viruses by trypsin treatmentVirology, 1975
- Studies on the formation of the influenza virus envelopeVirology, 1974
- The Polypeptides of Adenovirus-infected CellsJournal of General Virology, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- PHYSICAL AND BIOLOGICAL PROPERTIES OF INFLUENZA VIRUS COMPONENTS OBTAINED AFTER ETHER TREATMENTThe Journal of Experimental Medicine, 1960