C. Kohlmetz et al., IN-VITRO EXPRESSION OF A RECOMBINANT PARAMYOSIN OF ANCYLOSTOMA-CANINUM, International journal for parasitology, 28(8), 1998, pp. 1229-1233
The objective of this study was to characterise a recombinant antigen
of Ancylostoma caninum that had been identified by immunoscreening wit
h selected antisera described elsewhere. In vitro expression of clone
341 produced a protein with an apparent molecular mass of approximatel
y 34 kDa which was recognised in Western blots by antisera against who
le worms and antisera against esophagi from adult worms, but not by se
ra from experimentally infected dogs or rabbits. DNA sequencing showed
a cDNA of 1176 bp coding for a 34-kDa protein, similar to the size id
entified in the immunoblot. DNA database comparison revealed an 80-82%
homology with the Caenorhabditis elegans unc-15 gene coding for param
yosin. The deduced aa sequence of clone 341 showed 95% homology with t
he paramyosin aa sequence of C. elegans. Affinity purified antibodies
against the recombinant protein recognise a protein with an apparent m
olecular mass of 97 kDa of A. caninum muscle tissue fraction which is
in accordance with the molecular mass of paramyosin from Schistosoma m
ansoni and Schistosoma japonicum. (C) 1998 Australian Society for Para
sitology. Published by Elsevier Science Ltd.