Nucleoproteins of animal influenza viruses, in contrast to those of human strains, are not cleaved in infected cells.
We previously reported that nucleoproteins (NPs) of human influenza viruses are cleaved in infected cells and, as a result, two forms of NP, uncleaved (mol. wt. 56000) and cleaved (mol. wt. 53000) were accumulated late in infection. Here, we report that NPs of animal influenza viruses of non-human origin (isolated from pigs, equids , seals, whales, birds) exhibited proteolytic resistance in infected cells and did not undergo a change in mol. wt. in the course of infection. The resistance of the animal virus NPs to proteolytic cleavage was shown to be a virus-specific property and not the consequence of a low level of proteolysis in infected cells. Influenza A/H3N2 viruses isolated from swine in Hong Kong in 1976 were found to have a cleavable NP like that of 'human' viruses, supporting the hypothesis concerning the 'human' origin of these strains. The NP of human influenza virus (A/Aichi/2/68) adapted to an animal host (mouse) retained susceptibility to limited intracellular proteolysis. Thus, NP resistance to cleavage seems to be a stable viral characteristic enabling the NP56 ---- NP53 modification to be used as an indication of the origin of influenza viruses.
D000818:Animals; D002642:Chick Embryo; D006801:Humans; D009980:Influenza A virus / Q000378:metabolism*; D007251:Influenza, Human / Q000378:metabolism / Q000382:microbiology*; D009698:Nucleoproteins / Q000378:metabolism*; D009975:Orthomyxoviridae / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000032:analysis / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*; D014776:Virus Cultivation
D009698:Nucleoproteins; D010455:Peptides; D014764:Viral Proteins; D010447:Peptide Hydrolases