Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor

doi:10.1084/jem.177.2.465

This Article

	Full Text (PDF)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JEM
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Pontes de Carvalho, L. C.
	Articles by Nussenzweig, V.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Pontes de Carvalho, L. C.
	Articles by Nussenzweig, V.


Social Bookmarking

	What's this?

ARTICLES

Characterization of a novel trans-sialidase of Trypanosoma brucei procyclic trypomastigotes and identification of procyclin as the main sialic acid acceptor

LC Pontes de Carvalho, S Tomlinson, F Vandekerckhove, EJ Bienen, AB Clarkson, MS Jiang, GW Hart and V Nussenzweig
Department of Pathology, New York University Medical Center, New York 10016.

Here we report the presence of a trans-sialidase on the surface of Trypanosoma brucei culture-derived procyclic trypomastigotes. The enzyme is not detected in lysates of bloodstream trypomastigotes enriched for either stumpy or slender forms. The trans-sialidase catalyzes the transfer of alpha(2-3)-linked sialic acid residues to lactose. beta-galactopyranosyl residues are at least 100 times better acceptors for sialic acid than alpha-galactopyranosyl residues. In the absence of efficient acceptors, the purified enzyme transfers sialic acid to water, i.e., it acts as a sialidase. Although the T. cruzi and T. brucei trans-sialidases have very similar donor and acceptor specificities, they are antigenically distinct. Sodium dodecyl sulfate- polyacramide gel electrophoresis under nonreducing conditions and silver staining of the purified trans-sialidase reveals a single band of 63 kD. When the surface membrane of live procyclic trypomastigotes is trans-sialylated, using radioactive sialyllactose as the donor substrate, it appears that the only sialylated surface molecule is procyclin. Pronase treatment of live parasites removes only part of the surface sialic acid, in agreement with recent data showing that the glycosylphosphatidylinositol anchor of procyclin is sialylated (Ferguson, M. A. J., M. Murray, H. Rutherford, and M. J. McConville. 1993. Biochem. J. In press).
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

Guther, M. L. S., Lee, S., Tetley, L., Acosta-Serrano, A., Ferguson, M. A.J. (2006). GPI-anchored Proteins and Free GPI Glycolipids of Procyclic Form Trypanosoma brucei Are Nonessential for Growth, Are Required for Colonization of the Tsetse Fly, and Are Not the Only Components of the Surface Coat. Mol. Biol. Cell 17: 5265-5274 [Abstract] [Full Text]
Montagna, G. N., Donelson, J. E., Frasch, A. C. C. (2006). Procyclic Trypanosoma brucei Expresses Separate Sialidase and trans-Sialidase Enzymes on Its Surface Membrane. J. Biol. Chem. 281: 33949-33958 [Abstract] [Full Text]
Roper, J. R., Guther, M. L. S., MacRae, J. I., Prescott, A. R., Hallyburton, I., Acosta-Serrano, A., Ferguson, M. A. J. (2005). The Suppression of Galactose Metabolism in Procylic Form Trypanosoma brucei Causes Cessation of Cell Growth and Alters Procyclin Glycoprotein Structure and Copy Number. J. Biol. Chem. 280: 19728-19736 [Abstract] [Full Text]
Agusti, R., Paris, G., Ratier, L., Frasch, A. C.C., de Lederkremer, R. M. (2004). Lactose derivatives are inhibitors of Trypanosoma cruzi trans-sialidase activity toward conventional substrates in vitro and in vivo. Glycobiology 14: 659-670 [Abstract] [Full Text]
Nagamune, K., Acosta-Serrano, A., Uemura, H., Brun, R., Kunz-Renggli, C., Maeda, Y., Ferguson, M. A.J., Kinoshita, T. (2004). Surface Sialic Acids Taken from the Host Allow Trypanosome Survival in Tsetse Fly Vectors. J. Exp. Med. 199: 1445-1450 [Abstract] [Full Text]
Tiralongo, E., Schrader, S., Lange, H., Lemke, H., Tiralongo, J., Schauer, R. (2003). Two Trans-sialidase Forms with Different Sialic Acid Transfer and Sialidase Activities from Trypanosoma congolense. J. Biol. Chem. 278: 23301-23310 [Abstract] [Full Text]
Vassella, E., Butikofer, P., Engstler, M., Jelk, J., Roditi, I. (2003). Procyclin Null Mutants of Trypanosoma brucei Express Free Glycosylphosphatidylinositols on Their Surface. Mol. Biol. Cell 14: 1308-1318 [Abstract] [Full Text]
McConville, M. J., Mullin, K. A., Ilgoutz, S. C., Teasdale, R. D. (2002). Secretory Pathway of Trypanosomatid Parasites. Microbiol. Mol. Biol. Rev. 66: 122-154 [Abstract] [Full Text]
Acosta-Serrano, A., Cole, R. N., Mehlert, A., Lee, M. G.-S., Ferguson, M. A. J., Englund, P. T. (1999). The Procyclin Repertoire of Trypanosoma brucei. IDENTIFICATION AND STRUCTURAL CHARACTERIZATION OF THE GLU-PRO-RICH POLYPEPTIDES. J. Biol. Chem. 274: 29763-29771 [Abstract] [Full Text]