TY - JOUR
T1 - Molecular cloning of a gene encoding matrix metalloproteinase-like protein from Gnathostoma spinigerum
AU - Uparanukraw, P.
AU - Morakote, N.
AU - Harnnoi, T.
AU - Dantrakool, A.
N1 - Funding Information:
Acknowledgements This work was supported by a grant from the Thailand Research Fund (TRF). We thank Prof. Wanpen Chaicumpa of Mahidol University for providing us with the monoclonal antibody GN6/24. We also thank Drs. Nirbhay Ku-mar and Alan Scott of the Johns Hopkins University, School of Hygiene and Public Health, for valuable suggestions. Secretarial assistance by Ms. Angkana Pansomboon is also acknowledged.
Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 2001/8/14
Y1 - 2001/8/14
N2 - The advanced third-stage larvae (aL3) of Gnathostoma spinigerum contain a 24 kDa glycoprotein with diagnostic potential. Immunoscreening with the monoclonal antibody to the 24-kDa protein (mAb GN6/24) has identified a cDNA clone with an insert of 932 base pairs (bp). The insert contains a full-length gene of 732 bp encoding a protein that is 33-39% similar to matrix metalloproteinases (MMPs) of Caenorhabditis elegans and several lower and higher vertebrates. The MMP-like protein of G. spinigerum possesses the catalytic domain, but lacks the propeptide and hemopexin-like domains found in other MMPs. A signal peptide of 23 amino acids at its amino terminus indicates that it is a secretory protein, which is confirmed by Western blot analysis showing the presence of the 24 kDa protein in the excretory-secretory products of aL3.
AB - The advanced third-stage larvae (aL3) of Gnathostoma spinigerum contain a 24 kDa glycoprotein with diagnostic potential. Immunoscreening with the monoclonal antibody to the 24-kDa protein (mAb GN6/24) has identified a cDNA clone with an insert of 932 base pairs (bp). The insert contains a full-length gene of 732 bp encoding a protein that is 33-39% similar to matrix metalloproteinases (MMPs) of Caenorhabditis elegans and several lower and higher vertebrates. The MMP-like protein of G. spinigerum possesses the catalytic domain, but lacks the propeptide and hemopexin-like domains found in other MMPs. A signal peptide of 23 amino acids at its amino terminus indicates that it is a secretory protein, which is confirmed by Western blot analysis showing the presence of the 24 kDa protein in the excretory-secretory products of aL3.
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U2 - 10.1007/s004360100440
DO - 10.1007/s004360100440
M3 - Article
C2 - 11570561
AN - SCOPUS:0034896063
VL - 87
SP - 751
EP - 757
JO - Parasitology Research
JF - Parasitology Research
SN - 0932-0113
IS - 9
ER -
