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. 2003 Jun;41(6):2300-5.
doi: 10.1128/JCM.41.6.2300-2305.2003.

Studies of epidemiology and seroprevalence of bovine noroviruses in Germany

Y Deng  1 , C A Batten, B L Liu, P R Lambden, M Elschner, H Günther, P Otto, P Schnürch, W Eichhorn, W Herbst, I N Clarke
Affiliations

Studies of epidemiology and seroprevalence of bovine noroviruses in Germany

Y Deng et al. J Clin Microbiol. 2003 Jun.

Abstract

Jena virus (JV) is a bovine enteric calicivirus that causes diarrhea in calves. The virus is approximately 30 nm in diameter and has a surface morphology similar to the human Norwalk virus. The genome sequence of JV was recently described, and the virus has been assigned to the genus Norovirus of the family CALICIVIRIDAE: In the present study, the JV capsid gene encoded by open reading frame 2 was cloned into the baculovirus transfer vector pFastBac 1, and this was used to transform Escherichia coli to generate a recombinant bacmid. Transfection of insect cells with the recombinant baculovirus DNA resulted in expression of the JV capsid protein. The recombinant JV capsid protein undergoes self-assembly into virus-like particles (VLPs) similar to JV virions in size and appearance. JV VLPs were released into the cell culture supernatant, concentrated, and then purified by CsCl equilibrium gradient centrifugation. Purified JV VLPs were used to hyperimmunize laboratory animals. An antigen capture enzyme-linked immunosorbent assay (ELISA) was developed and characterized initially with clinical specimens containing defined human noroviruses and bovine diarrheal samples from calves experimentally infected with JV; the ELISA was specific only for JV. The ELISA was used to screen 381 diarrheal samples collected from dairy herds in Thuringia, Hesse, and Bavaria, Germany, from 1999 to 2002; 34 of these samples (8.9%) were positive for JV infection. The unexpectedly high prevalence of JV was confirmed in a seroepidemiological study using 824 serum or plasma samples screened using an anti-JV ELISA, which showed that 99.1% of cattle from Thuringia have antibodies to JV.

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Figures

FIG. 1.
FIG. 1.
SDS-polyacrylamide gel showing kinetics of JV capsid expression. Lane L contains molecular mass markers: bovine serum albumin (66 kDa), ovalbumin (45 kDa), glyceraldehyde-3-phosphate dehydrogenase (36 kDa), carbonic anhydrase (29 kDa), trypsinogen (24 kDa), trypsin inhibitor (20 kDa), and α-lactalbumin (14 kDa). Lanes 1 to 5 represent days 1 to 5 postinfection for cell culture supernatant and cells. The arrow indicates the JV capsid protein that is exported to the cell culture supernatant.
FIG. 2.
FIG. 2.
Electron micrograph of negatively stained JV VLPs. Bar, 50 nm.
FIG. 3.
FIG. 3.
Radioimmunoprecipitation of JV capsid protein produced by in vitro transcription-translation. The positions of the molecular mass markers are indicated on the left. Lane 1, preimmunization mouse serum; lane 2, postimmunization mouse serum; lane 3, preimmunization rabbit serum; lane 4, postimmunization rabbit serum. The position of the immunoprecipitated JV capsid protein at 55 kDa is indicated by the arrow.
FIG. 4.
FIG. 4.
Epidemiological screen for antibodies to JV. A total of 824 serum or plasma samples collected from 25 different dairy herds in Thuringia, Germany, between January and February 2002 were screened for antibodies against rJV VLPs. The OD450 was plotted against increasing age. Each diamond represents a serum or plasma OD450 value for a sample plotted against the age of the individual animal in weeks. Positive reactivity to JV capsid was confirmed by RIPA analysis of a selection of samples. All sera with OD450 values of <0.4 did not immunoprecipitate with JV capsid protein; thus, samples below this value were designated negative.
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