Identification and characterization of the major proteins of malignant catarrhal fever virus

H Li; D T Shen; W C Davis; D P Knowles; J R Gorham; T B Crawford

doi:10.1099/0022-1317-76-1-123

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Identification and characterization of the major proteins of malignant catarrhal fever virus

Journal article

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Peer reviewed

Identification and characterization of the major proteins of malignant catarrhal fever virus

H Li, D T Shen, W C Davis, D P Knowles, J R Gorham and T B Crawford

Journal of general virology, Vol.76 ( Pt 1)(1), pp.123-129

01/1995

DOI: https://doi.org/10.1099/0022-1317-76-1-123

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https://hdl.handle.net/2376/113159

PMID: 7844521

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Abstract

Immune Sera - immunology

Viral Proteins - immunology

Glycosylation

Precipitin Tests

Gammaherpesvirinae - chemistry

Animals

Malignant Catarrh - virology

Cattle

Sheep

Mice

Mice, Inbred BALB C

Antibodies, Monoclonal - immunology

Viral Proteins - analysis

Malignant catarrhal fever virus (MCFV), a gamma-herpesvirus, causes a severe inflammatory and lymphoproliferative disease of cattle and other susceptible ruminants. Polyclonal antisera and monoclonal antibodies (MAbs) to the Minnesota isolate of MCFV were produced and used to examine the characteristics of the viral proteins. Immunoprecipitation of antigens of the Minnesota isolate of MCFV with polyclonal antisera revealed at least 11 proteins with molecular masses ranging from 17 kDa to 145 kDa. Among 279 candidate anti-MCFV hybridomas, 14 were selected and clustered into six groups on the basis of the patterns of reactivity to viral proteins in immunoprecipitation and immunoblot. The group I MAbs exhibited strong neutralizing activity and recognized a glycosylation-dependent conformational epitope on a 110 kDa protein. The MAbs in group II bound a non-neutralizing conformational epitope on a 130 kDa non-glycosylated protein. A glycosylated protein complex of 115/110/105/78/45 kDa moieties was identified by the MAbs in group III. The MAbs in groups IV, V and VI reacted with non-glycosylated proteins of 36/34 kDa, 24 kDa and 17 kDa, respectively. Comparison of three MCFV isolates [the Minnesota isolate, the Austrian isolate (Au-732) and the African prototype isolate (WC-11)] revealed no apparent differences in immunoprecipitation patterns with the single exception that the 110 kDa protein of WC-11 was slightly smaller than its counterpart in the Minnesota isolate.

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Title: Identification and characterization of the major proteins of malignant catarrhal fever virus
Creators: H Li - Animal Diseases Research Unit, USDA Agricultural Research Service, Pullman, WA
D T Shen
W C Davis
D P Knowles
J R Gorham
T B Crawford
Publication Details: Journal of general virology, Vol.76 ( Pt 1)(1), pp.123-129
Academic Unit: Veterinary Microbiology and Pathology, Department of
Publisher: England
Identifiers: 99900547625001842
Language: English
Resource Type: Journal article