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J Gen Virol 70 (1989), 13-23; DOI 10.1099/0022-1317-70-1-13
© 1989 Society for General Microbiology
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A Novel Approach to the Serology of Potyviruses Involving Affinity-purified Polyclonal Antibodies Directed towards Virus-specific N Termini of Coat Proteins

D. D. Shukla1, J. Jilka2, M. Tosic4 and R. E. Ford3

1 CSIRO, Division of Biotechnology, Parkville Laboratory, 343 Royal Parade, Parkville, Victoria 3052, Australia
2 Department of Biochemistry
and3 Department of Plant Pathology, University of Illinois, Urbana, Illinois 61801, U.S.A.
and4 Faculty of Agriculture, University of Belgrade, Beograd-Zemun, 11080, Yugoslavia

Attempts to identify and classify distinct potyviruses and their strains have frequently been hampered by the presence of variable proportions of cross-reacting antibodies in antisera. Investigations of reactivities in electroblot immunoassays of 11 polyclonal antisera raised by injection of intact particles of potyviruses produced in different laboratories with 12 distinct potyviruses showed that such cross-reacting antibodies were directed towards the homologous core protein region of potyvirus coat proteins. A simple method was developed to obtain virus-specific antibodies using affinity chromatography. It involved removal of the surface-located, virus-specific N-terminal peptide region from particles of one potyvirus using lysyl endopeptidase, coupling of the truncated coat protein to cyanogen bromide-activated Sepharose gel, and passing antisera to different potyviruses through the column. Antibodies that did not bind to the column were found to be highly specific.

Keywords: potyviruses, coat proteins, serology

Received 9 May 1988; accepted 28 September 1988.




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Copyright © 1989 by the Society for General Microbiology.