Abstract
Recombinants between fowl plague virus (FPV, H7N1) and the Hong Kong (H3N2) or Singapore (H2N2) influenza virus strains carrying the hemagglutinin of FPV and the neuraminidase of the human strains form only very tiny plaques at 33°, but normal plaques at 37°. One recombinant (113/Ho) has been studied in more detail. It multiplies only very slowly at 33°, the nonpermissive temperature. Adsorption and penetration are normal at 33°, but synthesis of protein is impeded. Temperature-shift experiments suggest that the synthesis of viral mRNA is slowed at 33°. 113/Ho does not agglutinate chicken erythrocytes at 40°, as the parent viruses do. 113/Ho can be adapted to grow normally at 33°. The frequency of adaptation is comparable to reversion of a single point mutation (ca. 10−5). Recombinants which grow well at 37° but not at 33° are called cold-sensitive (cs) recombinants.
References
- Bosch F.X., Orlich M., Klenk H.-D., Rott R. The structure of the hemagglutinin, a determinant for the pathogenicity of influenza virus. Virology. 1979;95:197–207. doi: 10.1016/0042-6822(79)90414-8. [DOI] [PubMed] [Google Scholar]
- Klenk H.-D., Rott R., Becht H. On the structure of influenza virus envelope. Virology. 1972;47:579–591. doi: 10.1016/0042-6822(72)90547-8. [DOI] [PubMed] [Google Scholar]
- Koennecke I., Boschek C.B., Scholtissek C. Isolation and properties of a temperaturesensitive mutant (ts 412) of an influenza virus recombinant with a is lesion in the gene coding for the nonstructural protein. Virology. 1981;110:16–25. doi: 10.1016/0042-6822(81)90003-9. [DOI] [PubMed] [Google Scholar]
- Mahy B.W.J. Mutants of influenza virus. In: Palese P., Kingsbury D.W., editors. Genetics of Influenza Viruses. Springer-Verlag; Wien, N. Y: 1983. in press. [Google Scholar]
- Nakamura K., Homma M. Cell fusion by HeLa cells persistently infected with hemadsorption type 2 virus. J. Gen. Virol. 1974;25:117–124. doi: 10.1099/0022-1317-25-1-117. [DOI] [PubMed] [Google Scholar]
- Rott R., Orlich M., Scholtissek C. Correlation of pathogenicity and gene constellation of influenza A viruses. III. Non-pathogenic recombinants derived from highly pathogenic parent strains. J. Gen. Virol. 1979;44:471–477. doi: 10.1099/0022-1317-44-2-471. [DOI] [PubMed] [Google Scholar]
- Scholtissek C., Harms E., Rohde W., Orlich M., Rott R. Correlation between RNA fragments of fowl plaque virus and their corresponding gene functions. Virology. 1976;74:332–344. doi: 10.1016/0042-6822(76)90340-8. [DOI] [PubMed] [Google Scholar]
- Scholtissek C., Spring S.B. Suppressor recombinants and Suppressor mutants. In: Nayak D.P., editor. ICN-UCLA Symposia on Molecular and Cellular Biology XXI. Academic Press; New York/London/Toronto/Sydney/San Francisco: 1981. pp. 399–413. (Genetic Variation among Influenza Viruses). [Google Scholar]
- Seto J.T., Rott R. Functional significance of sialidase during influenza virus multiplication. Virology. 1966;30:731–737. doi: 10.1016/0042-6822(66)90178-4. [DOI] [PubMed] [Google Scholar]
- Somers K., Kit S. Vol. 70. 1973. Temperature-dependent expression of transformation by a cold-sensitive mutant of murine sarcoma virus; pp. 2206–2210. (Proc. Nat Acad Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stohlman S.A., Sakaguchi A.Y., Weiner L.P. Characterization of the cold-sensitive murine hepatitis virus mutants rescued from latently infected cells by cell fusion. Virology. 1979;98:448–455. doi: 10.1016/0042-6822(79)90567-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wright P.J., Cooper P.D. Isolation of cold-sensitive mutants of poliovirus. Intervirology. 1973;2:20–24. doi: 10.1159/000149400. [DOI] [PubMed] [Google Scholar]