Abstract
A zinc metalloendopeptidase cDNA ( Ac-mep-1) was cloned from Ancylostoma caninum adult hookworms. Ac-mep-1 is encoded by a 2.8 kb mRNA with a predicted open reading frame (ORF) of 870 amino acids (predicted pI=5.5, m.w.=98.7 kDa) that contains four potential N-linked glycosylation sites and predicted zinc-binding domains (HExxH and ENxADxGG). These domains represent signature sequences of the Neutral Endopeptidase 24.11 (neprilysin) family of enzymes. The ORF corresponding to Ac-MEP-1 exhibited strong similarity to metalloproteases from the trichostrongyle Haemonchus contortus as well as Caenorhabditis elegans. RT-PCR analysis of A. caninum eggs, L 1, non-activated and activated L 3 and adult cDNA identify transcription of Ac-MEP-1 only in the adult stage of the parasite. Mouse antibody raised to the expressed protein recognized proteins of ∼90 and 100 kDa in adult hookworm extracts. Adult worm sections probed with these antisera localized Ac- mep-1 to the microvilli of the worm gastrointestinal tract suggesting a possible role for this enzyme in digestion of the parasite blood meal.
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