Molecular cloning and characterization of Echinostoma caproni heat shock protein-70 and differential expression in the parasite derived from low- and high-compatible hosts.

Abstract:

:We cloned and expressed Echinostoma caproni HSP70 in Escherichia coli. This molecule presents an open reading frame (ORF) of 655 amino acids, and a theoretical molecular weight of 71 kDa. E. caproni HSP70 protein showed a high homology to other helminth molecules, major differences being located in the C-terminal region of the molecule, with a hydrophobic portion. Studies of protein and messenger RNA (mRNA) expression revealed a distinct pattern, depending on the host (low- or high-compatible). Specific polyclonal antisera raised against the recombinant protein expressed in Escherichia coli demonstrated its selective presence in excretory/secretory products (ESP) of adult parasites obtained from high-compatible hosts. Immunological studies showed clearly the association of HSP70 with the parasite surface and other structures, including eggs.

journal_name

Parasitology

journal_title

Parasitology

authors

Higón M,Monteagudo C,Fried B,Esteban JG,Toledo R,Marcilla A

doi

10.1017/S0031182008004927

subject

Has Abstract

pub_date

2008-10-01 00:00:00

pages

1469-77

issue

12

eissn

0031-1820

issn

1469-8161

pii

S0031182008004927

journal_volume

135

pub_type

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