Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (10)
Right arrowRequest Permissions
Right arrow Disclaimer
Citing Articles
Right arrowScopus Links
Google Scholar
Right arrow Articles by Hwa, K. Y.
Right arrow Articles by Englund, P. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hwa, K. Y.
Right arrow Articles by Englund, P. T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, Vol 9, 181-190, Copyright © 1999 by Oxford University Press

ORIGINAL ARTICLES

Protein glycosylation mutants of procyclic Trypanosoma brucei: defects in the asparagine-glycosylation pathway

KY Hwa, A Acosta-Serrano, KH Khoo, T Pearson and PT Englund
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

We employed a genetic approach to study protein glycosylation in the procyclic form of the parasite Trypanosoma brucei. Two different mutant parasites, ConA 1-1 and ConA 4-1, were isolated from mutagenized cultures by selecting cells which resisted killing or agglutination by concanavalin A. Both mutant cells show reduced concanavalin A binding. However, the mutants have different phenotypes, as indicated by the fact that ConA 1-1 binds to wheat germ agglutinin but ConA 4-1 and wild type do not. A blot probed with concanavalin A revealed that many proteins in both mutants lost the ability to bind this lectin, and the blots resembled one of wild type membrane proteins treated with PNGase F. This finding suggested that the mutants had altered asparagine- linked glycosylation. This conclusion was confirmed by studies on a flagellar protein (Fla1) and procyclic acidic repetitive protein (PARP). Structural analysis indicated that the N- glycan of wild type PARP is exclusively Man5GlcNAc2 whereas that in both mutants is predominantly a hybrid type with a terminal N- acetyllactosamine. The occupancy of the PARP glycosylation site in ConA 4-1 was much lower than that in ConA 1-1. These mutants will be useful for studying trypanosome glycosylation mechanisms and function.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Eukaryot CellHome page
S. Utz, I. Roditi, C. Kunz Renggli, I. C. Almeida, A. Acosta-Serrano, and P. Butikofer
Trypanosoma congolense Procyclins: Unmasking Cryptic Major Surface Glycoproteins in Procyclic Forms
Eukaryot. Cell, August 1, 2006; 5(8): 1430 - 1440.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Leal, A. Acosta-Serrano, J. Morris, and G. A. M. Cross
Transposon Mutagenesis of Trypanosoma brucei Identifies Glycosylation Mutants Resistant to Concanavalin A
J. Biol. Chem., July 9, 2004; 279(28): 28979 - 28988.
[Abstract] [Full Text] [PDF]

Home page
 Eukaryot CellHome page
A. Acosta-Serrano, J. O'Rear, G. Quellhorst, S. H. Lee, K.-Y. Hwa, S. S. Krag, and P. T. Englund
Defects in the N-Linked Oligosaccharide Biosynthetic Pathway in a Trypanosoma brucei Glycosylation Mutant
Eukaryot. Cell, April 1, 2004; 3(2): 255 - 263.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Acosta-Serrano, R. N. Cole, A. Mehlert, M. G.-S. Lee, M. A. J. Ferguson, and P. T. Englund
The Procyclin Repertoire of Trypanosoma brucei. IDENTIFICATION AND STRUCTURAL CHARACTERIZATION OF THE GLU-PRO-RICH POLYPEPTIDES
J. Biol. Chem., October 15, 1999; 274(42): 29763 - 29771.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Acosta-Serrano, E. Vassella, M. Liniger, C. K. Renggli, R. Brun, I. Roditi, and P. T. Englund
The surface coat of procyclic Trypanosoma brucei: Programmed expression and proteolytic cleavage of procyclin in the tsetse fly
PNAS, February 13, 2001; 98(4): 1513 - 1518.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.