trypanocidal Cape buffalo serum protein is xanthine oxidase

• Published in: Infection and Immunity Vol. 65; no. 9; pp. 3806 - 3814
• Main Authors: Muranjan, M, Wang, Q, Li, Y.L, Hamilton, E, Otieno-Omondi, F.P, Wang, J, Van Praagh, A, Grootenhuis, J.G, Black, S.J
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.09.1997
• Subjects: Africa; Amino Acid Sequence; animal health; animal parasites and pests; Animals; Antibiotics. Antiinfectious agents. Antiparasitic agents; Antiparasitic agents; Biological and medical sciences; Buffaloes - blood; Buffaloes - metabolism; Buffaloes - parasitology; Cattle; Cattle Diseases - enzymology; Cattle Diseases - parasitology; Fundamental and applied biological sciences. Psychology; Glycolysis; Hydrogen Peroxide - metabolism; Life cycle. Host-agent relationship. Pathogenesis; Medical sciences; Molecular Sequence Data; Pharmacology. Drug treatments; Protozoa; Tropical medicine; Trypanocidal Agents; Trypanosoma brucei; Trypanosoma brucei brucei - growth & development; Trypanosomiasis - veterinary; Xanthine Oxidase - blood; Africa; Kinetoplastida; Characterization; Protozoa; Antiprotozoal agent; Vertebrata; Mammalia; Purification; Trypanosoma; Artiodactyla; Serum protein; Ungulata
• ISSN: 0019-9567; 1098-5522
• DOI: 10.1128/IAI.65.9.3806-3814.1997

Plasma and serum from Cape buffalo (Syncerus caffer) kill bloodstream stages of all species of African trypanosomes in vitro. The trypanocidal serum component was isolated by sequential chromatography on hydroxylapatite protein A-G, Mono Q, and Superose 12. The purified trypanocidal protein had a molecular mass of 150 kDa, and activity correlated with the presence of a 146-kDa polypeptide detected upon reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino acid sequences of three peptide fragments of the 146-kDa reduced polypeptide, ligand affinity and immunoaffinity chromatography of the native protein, and sensitivity to pharmacological inhibitors, identified the trypanocidal material as xanthine oxidase (EC 1.1.3.22). Trypanocidal activity resulted in the inhibition of trypanosome glycolysis and was due to H2O2 produced during catabolism of extracellular xanthine and hypoxanthine by the purine catabolic enzyme.