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Purification and characterization of a metacestode cysteine proteinase from Taenia solium involved in the breakdown of human IgG

Published online by Cambridge University Press:  11 May 2005

S. BAIG ,
R. T. DAMIAN ,
J. L. MOLINARI ,
P. TATO ,
J. MORALES-MONTOR ,
M. WELCH ,
J. TALHOUK ,
R. HASHMEY  and
A. C. WHITE
S. BAIG
Affiliation:
Department of Cellular Biology, University of Georgia, Biological Sciences Building, Athens, GA 30603 Infectious Diseases Section, Department of Medicine, Baylor College of Medicine, 1 Baylor Plaza, 535EA, Houston, TX 77030, USA
R. T. DAMIAN
Affiliation:
Department of Cellular Biology, University of Georgia, Biological Sciences Building, Athens, GA 30603
J. L. MOLINARI
Affiliation:
Departamento de Genética Molecular, Instituto de Fisiología Celular, UNAM AP 70-242, México, DF 04510, México
P. TATO
Affiliation:
Departamento de Microbiología y Parasitología, Facultad de Medicina, UNAM, Av. Universidad 3000, DF 04510, México
J. MORALES-MONTOR
Affiliation:
Department of Cellular Biology, University of Georgia, Biological Sciences Building, Athens, GA 30603 Departamento de Inmunología, Instituto de Investigaciones Biomédicas, UNAM AP 70228, Mexico DF 04510, México
M. WELCH
Affiliation:
Department of Cellular Biology, University of Georgia, Biological Sciences Building, Athens, GA 30603
J. TALHOUK
Affiliation:
Enzyme Systems Products, Livermore, CA
R. HASHMEY
Affiliation:
Infectious Diseases Section, Department of Medicine, Baylor College of Medicine, 1 Baylor Plaza, 535EA, Houston, TX 77030, USA
A. C. WHITE
Affiliation:
Infectious Diseases Section, Department of Medicine, Baylor College of Medicine, 1 Baylor Plaza, 535EA, Houston, TX 77030, USA
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Abstract

Infection of the central nervous system by Taenia solium cysticerci is the cause of human neurocysticercosis, a major neurological infection in the Third World and an emerging infectious disease in the United States. We previously isolated a cysteine proteinase from cysticerci of Taenia crassiceps and demonstrated that it degrades human IgG in vitro. We have now isolated a 48 kDa thiol-dependent proteinase from T. solium. The T. solium enzyme also degrades human IgG, but does not significantly degrade albumin. IgG degradation was inhibited by cysteine proteinase inhibitors, but not significantly by inhibitors of aspartic, serine, or metalloproteinases. The peptide substrate specificity and pH optimum resemble cathepsin L. The Km for the peptide substrate Z-Phe-Arg-AFC was calculated to be 7·0×10−6M, the Kcat was 1·98×105 s−1, and the Kcat/Km 2·84×109M−1 s−1, a value which is within the diffusion control limit for highly catalytic enzymes. We propose that immunoglobulin degradation by the T. solium cysteine proteinase may play a key role in the host-parasite interface and could be employed as a target for chemotherapy.

Keywords

cysteine proteinaseTaenia soliumimmunoglobulinTaenia crassicepscysticercosis
Type
Research Article
Information
Parasitology , Volume 131 , Issue 3 , September 2005 , pp. 411 - 416
Copyright
© 2005 Cambridge University Press

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