viral hemorrhagic septicemia virus
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IdentityTop of page
Preferred Scientific Name
- viral hemorrhagic septicemia virus
International Common Names
- English: Egtved virus; viral haemorrhagic septicaemia virus
Taxonomic TreeTop of page
- Domain: Virus
- Unknown: "Positive sense ssRNA viruses"
- Unknown: "RNA viruses"
- Order: Mononegavirales
- Family: Rhabdoviridae
- Genus: Novirhabdovirus
- Species: viral hemorrhagic septicemia virus
Distribution TableTop of page
The distribution in this summary table is based on all the information available. When several references are cited, they may give conflicting information on the status. Further details may be available for individual references in the Distribution Table Details section which can be selected by going to Generate Report.
Pathogen CharacteristicsTop of page
Virus morphology and biochemistry
Viral hemorrhagic septicemia virus is placed within the family Rhabdoviridae in the Novirhabdovirus genus (Einer-Jensen, et al., 2004), because it is currently regarded as distant to viruses in the lyssavirus genus on genetic grounds (Wunner et al., 1995). The type species of Novirhabdovirus is infectious haematopoietic necrosis virus (IHNV). It is a bullet-shaped virus and, by electron microscopy, measures 70 nm width by 180 nm length. It is also enveloped, and the envelope contains the membrane glycoprotein, which is the major neutralizing surface antigen (Jørgensen et al., 1995). This is in common with other mammalian rhabdoviruses and the fish rhabdovirus IHNV (Luo et al., 1988; Benmansour et al., 1991; Huang, 1993).
Viral hemorrhagic septicemia virus is composed of a single-stranded ribonucleic acid (RNA) molecule, four structural proteins and the virion-associated polymerase (Lenoir and de Kinkelin, 1975; de Kinkelin et al., 1980; Benmansour et al., 1994). The structural proteins are the envelope glycoprotein (G), the nucleoprotein (N), the polymerase-associated protein (M1) and the matrix protein (M2). In addition, a non-virion (NV) protein is expressed in infected cells, but the function of this is not known (Schuetze et al., 1996; Kurath et al., 1997).
There have been no research studies on the assembly of the structural proteins of VHSV in relation to the nucleic acid. Knowledge of virus assembly for rhabdoviruses overall is derived from studies in particular on the type vesiculovirus, vesicular stomatitis virus (VSV), and the type lyssavirus, rabies virus (RV).
The RNA is helically wound and nucleoprotein has a close association with the RNA molecule, although the precise stabilizing forces have not been described. In RV, the internal matrix protein M1 is closely associated with the N protein (Prehaud et al., 1992) and in VSV the M1 protein is associated with the polymerase (L) protein (Banerjee and Barik, 1992). In VSV, the external matrix protein (M2) is closely associated with the nucleoprotein core structure (Wilson and Lenard, 1981) and the external envelope glycoprotein (G), which it stabilizes (Lyles et al., 1992).
Forms of the virus
In common with many RNA viruses with a negative-strand polarity genome, defective interfering (DI) particles are readily produced which are shorter and have a smaller RNA molecule than normal infectious particles. Such particles interfere with the standard complete infectious virus at the cellular level by competing for cell receptor binding sites and thereby blocking efficient replication of the standard full length virus (Wunner, 1985).
Serotypes and strains
Three serotypes of VHSV have been described: type 1, represented by strain F1 (Denmark), type 2, represented by the Heddedam isolate from Denmark, and type 3, represented by the French strain 23/75 isolated from brown trout by de Kinkelin and Le Berre (1977). These three serotypes were defined by a serum neutralization test. However, as Olesen et al. (1993) reported, there was considerable overlap of strains within and between these serotypes. These authors attempted to define more realistic serogroups, using cross-reacting polyclonal antiserum and four neutralizing monoclonal antibodies (MAbs). It was suggested that three serogroups were recognizable: serogroup I, neutralized by all four MAbs and the anti-F1 antibody, serogroup II, neutralized by only one MAb and the anti-F1 antibody, and serogroup III, not neutralized by any MAb but with low or no neutralization by the F1 antibody.
Although three serogroups were identified, Olesen et al. (1993) pointed out that 120 of 127 isolates were neutralized by an anti-F1 antiserum and these therefore showed common antigenic determinants. Serogroups were therefore in reality subtypes within a single serotype and the definition of the subtypes would be dependent on the MAbs used. What emerged from the study of newly classified VHS viruses by Olesen et al. (1993) was that there had been an antigenic shift from the period 1965-81 to 1992 in Denmark, by which the group I isolates, including F1 type isolate, had been largely displaced by new group II isolates in a single year from 1991 to 1992. What is known about new marine VHSV strains in European waters from cod and haddock in the North Sea and turbot from Gigha Island is that all the three neutralization serogroups are represented. It is also possible that the freshwater serotypes in Denmark had their origin in the marine environment.
In this connection, the glycoprotein gene sequence comparisons for a variety of marine and freshwater strains by Stone et al. (1997) are relevant. Phylogenetic analysis of a 360-nucleotide region of the G gene revealed three genogroups. Dendrograms based on the deduced amino acid sequence derived two genogroups. In genogroup II, strain 23-75 from brown trout in France, cod-79 (the first cod isolate from Denmark) and the Scottish Gigha turbot isolate (814) showed 100% homology for amino acid sequence. It was therefore postulated that these isolates from both fresh water and sea water shared a common evolution.
The recent review article (Einer-Jensen et al., 2004) points to a likely marine origin for the freshwater virulent isolates of VHS virus and synthesizes much of the available information in the literature. A previous paper by Thiery et al., (2003) reported G gene sequence information on historical French isolates from 1971 to 1999 and indicated a good correlation between the geographical origin of the isolates and their genetic characteristics. In another significant paper, Betts and Stone (2000) reported a complete genome sequence analysis of two virulent freshwater and two avirulent marine isolates, in a search for loci of virulence. As few as 10 amino acid substitutions were identically substituted between the freshwater and marine isolates, indicating a very limited number of amino acid substitutions may be required for a change of VHSV virulence for salmonids.
ReferencesTop of page
Banerjee AK, Barik S, 1992. Gene expression of vesicular stomatitis virus genome RNA. Virology, 188:417-428
Benmansour A, Paubert G, Bernard J, Kinkelin Pde, 1994. The polymerase-associated protein (M1) and the matrix protein (M2) from a virulent and an avirulent strain of viral hemorrhagic septicemia virus (VHSV), a fish rhabdovirus. Virology (New York), 198(2):602-612; 42 ref
Einer-Jensen K, Ahrens P, Forsberg R, Lorenzen N, 2004. Evolution of the fish rhabdovirus viral haemorrhagic septicaemia virus. Journal of General Virology. 85:1167-1179
Huang C, 1993. Mapping of antigenic sites of infectious hematopoietic necrosis virus glycoprotein. PhD thesis. Seattle, USA: University of Washington
Kinkelin Pde, Bearzotti-Le Berre M, Bernard J, 1980. Viral hemorrhagic septicemia of rainbow trout: selection of a thermoresistant virus variant and comparison of polypeptide synthesis with the wild-type virus strain. Journal of Virology, 36(3):652-658
Kinkelin Pde, Le Berre M, 1977. Isolement d’un rhabdovirus pathogène de la truite fario (Salmo trutta, L. 1766). Comptes Rendus Hebdomadaires des Séances, Académie des Sciences (Paris), 284:101-104
Luo L, Li Y, Snyder RM, Wagner RR, 1988. Point mutations in glycoprotein gene of vesicular stomatitis virus (New Jersey serotype) selected by resistance to neutralization by epitope-specific monoclonal antibodies. Virology, 163(2):341-348; 27 ref
Lyles DS, McKenzie M, Parce JW, 1992. Subunit interactions of vesicular stomatitis virus envelope glycoprotein stabilized by binding to viral matrix protein. Journal of Virology, 66(1):349-358; 24 ref
OIE Handistatus, 2005. World Animal Health Publication and Handistatus II (data set for 2004). Paris, France: Office International des Epizooties
Olesen NJ, Lorenzen N, J
Préhaud C, Nel K, Bishop DHL, 1992. Baculovirus-expressed rabies virus M1 protein is not phosphorylated: it forms multiple complexes with expressed rabies N protein. Virology (New York), 189(2):766-770; 12 ref
Schütze H, Enzmann PJ, Mundt E, Mettenleiter TC, 1996. Identification of the non-virion (NV) protein of fish rhabdoviruses viral haemorrhagic septicaemia virus and infectious haematopoietic necrosis virus. Journal of General Virology, 77(6):1259-1263
Stone DM, Way K, Dixon PF, 1997. Nucleotide sequence of the glycoprotein gene of viral haemorrhagic septicaemia (VHS) viruses from different geographical areas: a link between VHS in farmed fish species and viruses isolated from North Sea cod (Gadus morhua L.). Journal of General Virology, 78(6):1319-1326
Thiéry R, Boisséson Cde, Jeffroy J, Castric J, Kinkelin Pde, Benmansour A, 2003. Phylogenetic analysis of viral haemorrhagic septicaemia virus (VHSV) isolates from France (1971-1999). Diseases of Aquatic Organisms, 52(1):29-37
Wilson T, Lenard J, 1981. Interactions of wild type and mutant M protein of vesicular stomatitis virus with nucleocapsids in vitro. Biochemistry, 20:1349-1354
Wunner WH, 1985. Growth, purification and titration of rhabdoviruses. In: Mahy BWJ, ed. Virology, a Practical Approach. Oxford: IRL Press, 79-93
Wunner WH, Calisher CH, Dietzgen RG, Jackson AO, Kitajima EW, Lafon M, Leong JC, Nichol S, Peters D, Smith JS, Walker PJ, 1995. Family Rhabdoviridae. In: Murphy FA, Fauquet CM, Bishop DHL, Ghabrial SA, Jarvis AW, Martelli GP, Mayo MA, Summers MD, eds. Virus Taxonomy. Sixth Report of the International Committee on Taxonomy of Viruses. Archives of Virology, Supplement 10, 275-288
Distribution MapsTop of page
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