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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
Identification of a 33-kilodalton immunodominant antigen of Trypanosoma cangolense as acysteine protease
Molecular and Biochemical Parasitology, Volume 56, No. 1, Year 1992
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Description
A 33-kDa protein of Trypanosoma congolense is a major antigen in infected cattle and the production of antibody to this antigen appeared to correlate with enhanced resistance to trypanosomiasis [4]. Immunoelectron microscopy using a monoclonal antibody (mAb 4C5) raised against the 33-kDa antigen showed a lysosomal localisation, similar to that of a previously described 32-kDa cysteine protease of T. congolense. Both mAb 4C5 and anti-33 kDa antibody from infected cattle bound on Western blots to the cysteine protease that had been purified by affinity chromatography on cystatin-Sepharose. Sepharose-coupled mAb 4C5 was used to affinity purify the antigen from bloodstream forms of T. congolense. On sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), the affinity-purified antigen had a molecular mass of 33 kDa under non-reducing conditions, and 40 kDa under reducing conditions. Anti-33-kDa antibody from infected cattle bound to both non-reduced and reduced affinity-purified antigen on Western blots. Serum from a rabbit immunised with the biochemically purified enzyme also bound the affinity-purified antigen. The affinity-purified antigen displayed proteolytic activity in fibrinogen-containing SDS-PAGE and against Azocoll. It hydrolysed benzyloxycarbonyl-Phe-Arg-7-amino-methyl coumarin (Z-Phe-Arg-NHMec) with a Km similar to that of the biochemically purified enzyme. Proteolytic and peptidolytic activities of the antigen were inhibited by the inhibitors of cysteine proteases, cystatin and trans-epoxysuccinyl-l-leucyl-amido (4-guanidino)butane (E-64). On two-dimensional gel electrophoresis, the antigen displayed similar characteristics to those of the biochemically purified enzyme. We conclude that the 33-kDa antigen of T. congolense and the cysteine protease are the same molecule. © 1992.
Authors & Co-Authors
Authiè, Édith
Kenya, Nairobi
International Laboratory for Research on Animal Diseases, Kenya
Muteti, David K.
Kenya, Nairobi
International Laboratory for Research on Animal Diseases, Kenya
Mbawa, Zeres R.
Kenya, Nairobi
International Laboratory for Research on Animal Diseases, Kenya
Lonsdale-Eccles, John David
Kenya, Nairobi
International Laboratory for Research on Animal Diseases, Kenya
Webster, Paul J.
Kenya, Nairobi
International Laboratory for Research on Animal Diseases, Kenya
Wells, Clive W.
Kenya, Nairobi
International Laboratory for Research on Animal Diseases, Kenya
Statistics
Citations: 65
Authors: 6
Affiliations: 1
Identifiers
Doi:
10.1016/0166-6851(92)90158-G
ISSN:
01666851