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Journal of Virology, December 2002, p. 12646-12653, Vol. 76, No. 24
0022-538X/02/$04.00+0 DOI: 10.1128/JVI.76.24.12646-12653.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Jorge L. Martínez-Torrecuadrada,2,
Fernando Roncal,1 Elvira Domínguez,1 and Juan Antonio García1*
Centro Nacional de Biotecnología (C.S.I.C.), Campus de la Universidad Autónoma de Madrid, 28049 Madrid,1 Ingenasa, 28037 Madrid, Spain2
Received 5 July 2002/ Accepted 13 September 2002
PEPSCAN analysis has been used to characterize the immunogenic regions of the capsid protein (CP) in virions of plum pox potyvirus (PPV). In addition to the well-known highly immunogenic N- and C-terminal domains of CP, regions within the core domain of the protein have also shown high immunogenicity. Moreover, the N terminus of CP is not homogeneously immunogenic, alternatively showing regions frequently recognized by antibodies and others that are not recognized at all. These results have helped us to design efficient antigen presentation vectors based on PPV. As predicted by PEPSCAN analysis, a small displacement of the insertion site in a previously constructed vector, PPV-
, turned the derived chimeras into efficient immunogens. Vectors expressing foreign peptides at different positions within a highly immunogenic region (amino acids 43 to 52) in the N-terminal domain of CP were the most effective at inducing specific antibody responses against the foreign sequence.
Present address: Centre for Protein Engineering-MRC, Cambridge CB2 2QH, United Kingdom.
Present address: Biotechnology Programme, Spanish National Cancer Center (CNIO), 28029 Madrid, Spain.
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