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
Parasitologyjournal_title
Parasitologyauthors
Higón M,Monteagudo C,Fried B,Esteban JG,Toledo R,Marcilla Adoi
10.1017/S0031182008004927subject
Has Abstractpub_date
2008-10-01 00:00:00pages
1469-77issue
12eissn
0031-1820issn
1469-8161pii
S0031182008004927journal_volume
135pub_type
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