Trypanosoma rangeli sialidase lacks trans-sialidase activity.
Extracts and tissue culture supernatants of axenic forms of T. rangeli were assayed for the presence of sialidase and trans-sialidase activities. Using sialyl(alpha 2-3)lactose, sialyl(alpha 2-6)lactose, poly(alpha 2-8)N-acetylneuraminic acid, fetuin and 4-methylumbelliferyl-N-acetylneuraminic acid as sialic acid donors, and lactose as a sialic acid acceptor, no trans-sialidase activity was detected. Nevertheless, T. rangeli lysates and culture supernatants contain a sialidase that hydrolyzes sialyl(alpha 2-3)lactose, and much less efficiently sialyl(alpha 2-6)lactose, but not poly(alpha 2-8)N-acetylneuraminic acid. T. cruzi trans-sialidase hydrolyzed only sialyl(alpha 2-3)lactose under the same conditions. The T. rangeli and the T. cruzi enzymes differ antigenically and in their pH optimum for hydrolase activity.
Pontes-de-Carvalho
L C
LC
Department of Pathology, New York University Medical Center, NY 10016.
Tomlinson
S
S
Nussenzweig
V
V
D000818:Animals; D000953:Antigens, Protozoan; D006023:Glycoproteins; D006863:Hydrogen-Ion Concentration; D007120:Immunochemistry; D009439:Neuraminidase / Q000276:immunology / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism; D013045:Species Specificity; D013379:Substrate Specificity; D014345:Trypanosoma / Q000201:enzymology* / Q000276:immunology; D014346:Trypanosoma brucei brucei / Q000201:enzymology / Q000276:immunology; D014349:Trypanosoma cruzi / Q000201:enzymology / Q000276:immunology
D000953:Antigens, Protozoan; D006023:Glycoproteins; D012794:Sialic Acids; C069715:trans-sialidase; D009439:Neuraminidase