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The application of mass spectrometry to identify immunogenic components of excretory/secretory products from adult Dictyocaulus viviparus

Published online by Cambridge University Press:  12 May 2005

J. B. MATTHEWS ,
A. J. DAVIDSON  and
R. J. BEYNON
J. B. MATTHEWS
Affiliation:
Division of Parasitology, Moredun Research Institute, Pentlands Science Park, Midlothian, EH26 0PZ
A. J. DAVIDSON
Affiliation:
Department of Veterinary Preclinical Science, Faculty of Veterinary Science, University of Liverpool, Crown Street, Liverpool, L69 7JZ
R. J. BEYNON
Affiliation:
Department of Veterinary Preclinical Science, Faculty of Veterinary Science, University of Liverpool, Crown Street, Liverpool, L69 7JZ
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Abstract

Proteomics has come to the forefront in the post-genomic era. The ability to compare and identify proteins expressed in a particular cell type under specific physiological or pathological states requires a range of technologies, including separation of complex protein or peptide mixtures, densitometry-based or isotope-coded methods for comparison of multiple proteomes, and mass spectrometric methods for identification of individual low abundance proteins. Although an emergent technology, thus far, proteomics has provided new perspectives on many problems in biomedical science. In parasitology, proteomics has been used to answer specific biological questions relating to survival and development, and also to identify candidates for vaccines. Here, we describe an ongoing research programme in which proteomics is being used to identify potential vaccine candidates for the bovine lungworm, Dictyocaulus viviparus. This work is focusing on antibody responses to the adult parasite excretory/secretory (ES) products, with selection of candidate antigens based on differential screening with serum from immune versus non-immune animals to simplify the proteome and the ensuing analytical challenges. Thus far, we have identified seven candidate proteins using this strategy. Of these, one protein showed significant identity to a previously cloned gene from D. viviparus, whilst the other six proteins have shown no significant identities. Isolation of further peptide sequences is now warranted to facilitate cloning of the genes encoding these antigens.

Keywords

Dictyocaulus viviparusantibody responsesproteomicsmass spectrometry
Type
Research Article
Information
Parasitology , Volume 128 , Issue S1 , October 2004 , pp. S43 - S47
Copyright
© 2004 Cambridge University Press

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