AI Article Synopsis
- A cDNA for a potential tissue inhibitor of metalloprotease (Ac-TMP) was isolated from an Ancylostoma caninum hookworm library using immunoscreening methods.
- Ac-TMP is a 140-amino acid protein with specific structural features similar to human TIMP-2, showing 33% identity and 50% similarity.
- Transcription of the Ac-tmp gene occurs only in the adult stage of the hookworm, and it's one of the most abundant proteins found in the secretions of this parasite, marking it as the first reported TIMP from a parasitic invertebrate.
Article Abstract
A cDNA encoding a putative tissue inhibitor of metalloprotease was cloned from an Ancylostoma caninum adult hookworm cDNA library by immunoscreening with anti-hookworm secretory products antiserum. Ac-TMP (A. caninum tissue inhibitor of metalloproteinase) is encoded by a 480-bp mRNA with a predicted open reading frame of 140 amino acids (molecular weight, 16,100 Da) that contains one potential N-linked glycosylation site and an N-terminal Cys-X-Cys consensus sequence. The open reading frame corresponds to a putative hookworm tissue inhibitor of metalloproteases (TIMP) with 33% identity and 50% similarity to the N-terminal domain of human TIMP-2. Analysis by reverse transcriptase-polymerase chain reaction indicates that transcription of Ac-tmp is restricted to the adult stage. The protein was isolated from A. caninum adult secretory products by reverse-phase high-performance liquid chromatography and identified as one of the most abundant proteins released by the parasite. To our knowledge, this is the first description of a TIMP from a parasitic invertebrate.
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| http://dx.doi.org/10.4269/ajtmh.2002.66.238 | DOI Listing |
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