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Molecular characterization and expression of two putative protective excretory secretory proteins of Haemonchus contortus.

Abstract：

:It has been shown that vaccination with two low molecular mass excretory secretory (ES) antigens of 15 and 24 kDa, respectively, afforded a substantial degree of protection against Haemonchus contortus to sheep. In vitro cultivation of the parasite usually yields a limited amount of these proteins and therefore, recombinant DNA technology was employed to clone the cDNAs encoding the ES proteins of interest and to express them in a convenient vector system. The N-terminal amino acid sequences of the two ES products were determined. Specific 5' primers were used in combination with an oligo (dT) 3' primer to amplify the appropriate cDNAs by polymerase chain reaction (PCR). A lambda ZAPII cDNA library was constructed from mRNA of L5 larvae and subsequently screened with the PCR products. The full length clone of the 15 kDa ES protein coded for a 17.2 kDa precursor molecule of 148 amino acids with a signal peptide of 30 amino acids. The full length clone of the 24 kDa ES protein coded for a 24.6 kDa precursor protein of 222 amino acids with a leader sequence of 19 residues. The expression of both ES products appeared to be developmentally regulated; mRNA encoding occurs only in the parasitic life stages. A cDNA of each ES protein was sub-cloned, without the leader sequence, into a pQE9 expression vector. Both purified recombinant proteins were recognized by sera from H. contortus hyperimmunised sheep as judged by immunoblot analysis, suggesting that antigenic determinants were also present on the recombinant proteins.

journal_name

Mol Biochem Parasitol

journal_title

Molecular and biochemical parasitology

authors

Schallig HD,van Leeuwen MA,Verstrepen BE,Cornelissen AW

doi

10.1016/s0166-6851(97)00093-5

subject

Has Abstract

pub_date

1997-09-01 00:00:00

pages

203-13

issue

1-2

eissn

0166-6851

issn

1872-9428

pii

S0166-6851(97)00093-5

journal_volume

88

pub_type

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