HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by de Turiso, J. A. L. Articles by Casal, J. I. Search for Related Content PubMed PubMed Citation Articles by de Turiso, J. A. L. Articles by Casal, J. I. Agricola Articles by de Turiso, J. A. L. Articles by Casal, J. I.

Fine mapping of canine parvovirus B cell epitopes

INGENASA, Inmunologia y Genetica Aplicada, S.A., Hermanos Garcia Noblejas, 41-2°, 28037 Madrid, Spain

In this report we describe the topological mapping of neutralizing domains of canine parvovirus (CPV). We obtained 11 CPV-specific monoclonal antibodies (MAbs), six of which are neutralizing. The reactivities were as determined by ELISA and Western blot (immunoblot) analysis. VP2, the most abundant protein of the CPV capsid, seemed to contain all the neutralization sites. Also, an almost full-length genomic clone of CPV was constructed in the bacterial plasmid pUC18 to enable expression of CPV proteins. All the neutralizing MAbs recognized recombinant VP2 when it was expressed as a free protein in Escherichia coli but not when expressed as a fusion protein with glutathione-S-transferase. When two large fragments containing about 85% and 67% of the C terminus of VP2 were expressed, no neutralization sites were detected. When fusion proteins containing the N terminus were expressed, two linear determinants were mapped, one between residues 1 to 10 of VP2, and the other between amino acids 11 and 23. The peptide 11 GQPAVRNERATGS 23, recognized by MAb 3C9, was synthesized chemically and checked for immunogenicity, not being able to induce neutralizing activity. Although the antibody response in rabbits to all the fusion proteins was uniformly high, the anti-CPV response was very variable. Protein from pCPVEx11, which contains a T cell epitope (peptide PKIFINLAKKKKAG) present in the VP1-specific region as well as the B cell epitopes, seemed to be the most effective in inducing virus neutralization.

Received 2 January 1991; accepted 11 June 1991.

This article has been cited by other articles:

				M. Nakamura, K. Nakamura, T. Miyazawa, Y. Tohya, M. Mochizuki, and H. Akashi Monoclonal Antibodies That Distinguish Antigenic Variants of Canine Parvovirus Clin. Vaccine Immunol., November 1, 2003; 10(6): 1085 - 1089. [Abstract] [Full Text] [PDF]

				M. R. Fernandez-Fernandez, J. L. Martinez-Torrecuadrada, F. Roncal, E. Dominguez, and J. A. Garcia Identification of Immunogenic Hot Spots within Plum Pox Potyvirus Capsid Protein for Efficient Antigen Presentation J. Virol., November 13, 2002; 76(24): 12646 - 12653. [Abstract] [Full Text] [PDF]

				M. E. Bloom, S. M. Best, S. F. Hayes, R. D. Wells, J. B. Wolfinbarger, R. McKenna, and M. Agbandje-McKenna Identification of Aleutian Mink Disease Parvovirus Capsid Sequences Mediating Antibody-Dependent Enhancement of Infection, Virus Neutralization, and Immune Complex Formation J. Virol., November 15, 2001; 75(22): 11116 - 11127. [Abstract] [Full Text] [PDF]