Skip to main content
Journal of Virology logoLink to Journal of Virology
. 1997 Dec;71(12):9016–9023. doi: 10.1128/jvi.71.12.9016-9023.1997

Characterization of infectious salmon anemia virus, an orthomyxo-like virus isolated from Atlantic salmon (Salmo salar L.).

K Falk 1, E Namork 1, E Rimstad 1, S Mjaaland 1, B H Dannevig 1
PMCID: PMC230202  PMID: 9371558

Abstract

Infectious salmon anemia (ISA) virus is the cause of infectious salmon anemia in farmed Atlantic salmon. The virus has been shown to contain RNA with structural characteristics similar to those of accepted members of the Orthomyxoviridae. Further biochemical, physiochemical, and morphological characterization of ISA virus was undertaken to clarify its taxonomic position. The virus was found to be sensitive to chloroform, heat, and low pH and agglutinated erythrocytes from fish. Erythrocytes from mammals or birds were not agglutinated. Receptor-destroying enzyme activity was detected, and the nature of this enzyme was suggested to be an acetylesterase. The buoyant density of the virus was 1.18 g/ml in sucrose and CsCl gradients. The maximum rate of virus replication was observed at 15 degrees C, while no virus was produced at 25 degrees C. Actinomycin D inhibited viral replication, and viral antigen was detected in nuclei by immunofluorescence. The addition of trypsin to the culture medium during virus replication had a beneficial effect on virus replication. ISA virus contains four major polypeptides with estimated molecular sizes of 71, 53, 43, and 24 kDa. Electron microscopy revealed structures closely resembling the nucleocapsids of influenza virus. Mushroom-shaped surface projections were a distinctive morphological feature, which differed from the rod-shaped hemagglutinin projections of the influenza viruses. The data reported here support the relationship of ISA virus to the Orthomyxoviridae, although ISA virus differs from influenza viruses in some morphological characteristics and in showing restricted hemagglutination, in different specificity of the receptor-destroying enzyme, in different polypeptide profile, in being unable to replicate at temperatures above 25 degrees C, and in host range.

Full Text

The Full Text of this article is available as a PDF (1.0 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arora D. J., Tremblay P., Bourgault R., Boileau S. Concentration and purification of influenza virus from allantoic fluid. Anal Biochem. 1985 Jan;144(1):189–192. doi: 10.1016/0003-2697(85)90103-4. [DOI] [PubMed] [Google Scholar]
  2. Compans R. W., Content J., Duesberg P. H. Structure of the ribonucleoprotein of influenza virus. J Virol. 1972 Oct;10(4):795–800. doi: 10.1128/jvi.10.4.795-800.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dannevig B. H., Falk K., Namork E. Isolation of the causal virus of infectious salmon anaemia (ISA) in a long-term cell line from Atlantic salmon head kidney. J Gen Virol. 1995 Jun;76(Pt 6):1353–1359. doi: 10.1099/0022-1317-76-6-1353. [DOI] [PubMed] [Google Scholar]
  4. Evensen O., Thorud K. E., Olsen Y. A. A morphological study of the gross and light microscopic lesions of infectious anaemia in Atlantic salmon (Salmo salar). Res Vet Sci. 1991 Sep;51(2):215–222. doi: 10.1016/0034-5288(91)90017-i. [DOI] [PubMed] [Google Scholar]
  5. GOTTSCHALK A. Neuraminidase: the specific enzyme of influenza virus and Vibrio cholerae. Biochim Biophys Acta. 1957 Mar;23(3):645–646. doi: 10.1016/0006-3002(57)90389-x. [DOI] [PubMed] [Google Scholar]
  6. HOLTERMANN O. A., HILLIS W. D., MOFFAT M. A. The development of soluble (S) and viral (V) antigens of influenza A virus in tissue culture as studied by the fluorescent antibody technique. 1. Studies employing a low multiplicity of infection in beef embryo kidney cells. Acta Pathol Microbiol Scand. 1960;50:398–408. doi: 10.1111/j.1699-0463.1960.tb01209.x. [DOI] [PubMed] [Google Scholar]
  7. Herrler G., Rott R., Klenk H. D., Müller H. P., Shukla A. K., Schauer R. The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase. EMBO J. 1985 Jun;4(6):1503–1506. doi: 10.1002/j.1460-2075.1985.tb03809.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hoffman G. L., Dunbar C. E., Wolf K., Zwillenberg L. O. Epitheliocystis, a new infectious disease of the bluegill (Lepomis macrochirus). Antonie Van Leeuwenhoek. 1969;35(2):146–158. doi: 10.1007/BF02219125. [DOI] [PubMed] [Google Scholar]
  9. Jennings P. A., Finch J. T., Winter G., Robertson J. S. Does the higher order structure of the influenza virus ribonucleoprotein guide sequence rearrangements in influenza viral RNA? Cell. 1983 Sep;34(2):619–627. doi: 10.1016/0092-8674(83)90394-x. [DOI] [PubMed] [Google Scholar]
  10. Kendal A. P. A comparison of "influenza C" with prototype myxoviruses: receptor-destroycing activity (neuraminidase) and structural polypeptides. Virology. 1975 May;65(1):87–99. doi: 10.1016/0042-6822(75)90009-4. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Lannan C. N., Winton J. R., Fryer J. L. Fish cell lines: establishment and characterization of nine cell lines from salmonids. In Vitro. 1984 Sep;20(9):671–676. doi: 10.1007/BF02618871. [DOI] [PubMed] [Google Scholar]
  13. Mjaaland S., Rimstad E., Falk K., Dannevig B. H. Genomic characterization of the virus causing infectious salmon anemia in Atlantic salmon (Salmo salar L.): an orthomyxo-like virus in a teleost. J Virol. 1997 Oct;71(10):7681–7686. doi: 10.1128/jvi.71.10.7681-7686.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Nagabayashi T., Wolf K. Characterization of EV-2, a Virus Isolated from European Eels (Anguilla anguilla) with Stomatopapilloma. J Virol. 1979 Apr;30(1):358–364. doi: 10.1128/jvi.30.1.358-364.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rogers G. N., Herrler G., Paulson J. C., Klenk H. D. Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J Biol Chem. 1986 May 5;261(13):5947–5951. [PubMed] [Google Scholar]
  16. Schauer R., Reuter G., Stoll S., Posadas del Rio F., Herrler G., Klenk H. D. Isolation and characterization of sialate 9(4)-O-acetylesterase from influenza C virus. Biol Chem Hoppe Seyler. 1988 Oct;369(10):1121–1130. doi: 10.1515/bchm3.1988.369.2.1121. [DOI] [PubMed] [Google Scholar]
  17. Vlasak R., Krystal M., Nacht M., Palese P. The influenza C virus glycoprotein (HE) exhibits receptor-binding (hemagglutinin) and receptor-destroying (esterase) activities. Virology. 1987 Oct;160(2):419–425. doi: 10.1016/0042-6822(87)90013-4. [DOI] [PubMed] [Google Scholar]
  18. WOLF K., QUIMBY M. C. Established eurythermic line of fish cells in vitro. Science. 1962 Mar 23;135(3508):1065–1066. doi: 10.1126/science.135.3508.1065. [DOI] [PubMed] [Google Scholar]
  19. Wolf K., Gravell M., Malsberger R. G. Lymphocystis virus: isolation and propagation in centrarchid fish cell lines. Science. 1966 Feb 25;151(3713):1004–1005. doi: 10.1126/science.151.3713.1004. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES