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Sequence, expression and localization of calmodulin-domain protein kinases in Eimeria tenella and Eimeria maxima

Published online by Cambridge University Press:  06 April 2009

P. P. J. Dunn
Affiliation:
Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, UK
J. M. Bumstead
Affiliation:
Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, UK
F. M. Tomley*
Affiliation:
Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, UK
*
*Corresponding author. Tel: + 44 1635 577276. Fax: + 44 635 577263. E-mail: Tomley@bbsrc.ac.uk.

Summary

We have isolated and sequenced cDNA clones from Eimeria tenella and Eimeria maxima which encode proteins that share homology with a recently described family of calmodulin-domain protein kinases. The primary sequence data show that each of the protein kinases can be divided into 2 main functional domains – an amino-terminal catalytic domain typical of serine/threonine protein kinases and a carboxy-terminal domain homologous to calmodulin, which is capable of binding calcium ions at 4 ‘EF-hand’ motifs. Expression of the E. tenella calmodulin-domain protein kinase (EtCDPK) increased towards the end of oocyst sporulation, as judged by Northern and Western blotting, and indirect immunofluorescent antibody labelling showed that within a few minutes of adding sporozoites to target host cells in in vitro culture EtCDPK was found to be specifically associated with a filament-like structure that converges at the apical end of the parasite. Once the parasite entered the host cell EtCDPK appeared to be left on the host cell membrane at the point of entry, indicating a brief yet specific role for this molecule in the invasion of host cells by E. tenella.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1996

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