Molecular cloning and purification of Ac-TMP, a developmentally regulated putative tissue inhibitor of metalloprotease released in relative abundance by adult Ancylostoma hookworms.

Bin Zhan Department of Microbiology and Tropical Medicine, George Washington University Medical Center and Albert B Sabin Vaccine Institute, Washington, District of Columbia 20037, USA.

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Mahnaz Badamchian Department of Microbiology and Tropical Medicine, George Washington University Medical Center and Albert B Sabin Vaccine Institute, Washington, District of Columbia 20037, USA.

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Bo Meihua Department of Microbiology and Tropical Medicine, George Washington University Medical Center and Albert B Sabin Vaccine Institute, Washington, District of Columbia 20037, USA.

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James Ashcom Department of Microbiology and Tropical Medicine, George Washington University Medical Center and Albert B Sabin Vaccine Institute, Washington, District of Columbia 20037, USA.

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Jianjun Feng Department of Microbiology and Tropical Medicine, George Washington University Medical Center and Albert B Sabin Vaccine Institute, Washington, District of Columbia 20037, USA.

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John Hawdon Department of Microbiology and Tropical Medicine, George Washington University Medical Center and Albert B Sabin Vaccine Institute, Washington, District of Columbia 20037, USA.

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Xiao Shuhua Department of Microbiology and Tropical Medicine, George Washington University Medical Center and Albert B Sabin Vaccine Institute, Washington, District of Columbia 20037, USA.

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Peter J Hotez Department of Microbiology and Tropical Medicine, George Washington University Medical Center and Albert B Sabin Vaccine Institute, Washington, District of Columbia 20037, USA.

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DOI:
https://doi.org/10.4269/ajtmh.2002.66.238
Volume/Issue:
Volume 66: Issue 3
Page(s):
238–244
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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.

Published Online:
Mar 2002
Cover The American Journal of Tropical Medicine and Hygiene
The American Journal of Tropical Medicine and Hygiene
Print ISSN:
0002-9637
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