This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow An erratum has been published
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zheng, L.
Right arrow Articles by Minocha, H. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zheng, L.
Right arrow Articles by Minocha, H. C.

 Previous Article  |  Next Article 

Clinical and Diagnostic Laboratory Immunology, March 2001, p. 283-287, Vol. 8, No. 2
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.2.283-287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Differentiation of Two Bovine Lentiviruses by a Monoclonal Antibody on the Basis of Epitope Specificity†

Ling Zheng,1 Shucheng Zhang,2 Charles Wood,3 Sanjay Kapil,1 Graham E. Wilcox,4 Thomas A. Loughin,5 and H. C. Minocha1,*

Departments of Diagnostic Medicine/Pathobiology1 and Statistics,5 Kansas State University, Manhattan, Kansas 66506; Intervet Incorporation, Millsboro, Delaware 199662; School of Biological Sciences, University of Nebraska, Lincoln, Nebraska 685883; and School of Veterinary Studies, Murdoch University, Murdoch 6150, Australia4

Received 20 September 2000/Returned for modification 2 November 2000/Accepted 28 November 2000

Bovine immunodeficiency virus (BIV) and Jembrana disease virus (JDV) are bovine lentiviruses that are closely related genetically. A recombinant fusion protein containing the capsid protein of BIV expressed in Escherichia coli was used to immunize mice and produce monoclonal antibodies. Six hybridomas specific for BIV capsid protein were identified, and one antibody, designated 10H1, was characterized further. Competitive binding assays were performed to analyze the topography of antigenic determinants by enzyme-linked immunosorbent assay and demonstrated the existence of at least three distinct antigenic determinants on capsid protein. The monoclonal antibody reacted specifically with both BIV capsid and the recombinant fusion protein in Western immunoblot analyses. However, it did not react with the recombinant capsid fusion protein of JDV, indicating that BIV contains at least one unique epitope in the capsid protein that is absent in JDV. Further mapping of the epitope by chemical cleavage analysis identified that the epitope is located at the 6.4-kDa N terminus of the 29-kDa capsid protein. This monoclonal antibody assay will be valuable for distinguishing the two closely related lentiviruses by Western blotting.

* Corresponding author: Mailing address: Department of Diagnostic Medicine/Pathobiology, College of Veterinary Medicine, 1800 Denison Ave. Kansas State University, Manhattan, KS 66506. Phone: (785) 532-4603, Fax: (786) 532-4039. E-mail: Minocha{at}vet.ksu.edu.

dagger Contribution 00-362-J from the Kansas Agricultural Experiment Station.

Clinical and Diagnostic Laboratory Immunology, March 2001, p. 283-287, Vol. 8, No. 2
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.2.283-287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.




Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»