scholarly journals The Major Surface Glycoprotein Expression Sites of Two Special Forms of RatPneumocystis cariniiDiffer in Structure

2000 ◽  
Vol 181 (5) ◽  
pp. 1729-1739 ◽  
Author(s):  
Joshua K. Schaffzin ◽  
James R. Stringer
Keyword(s):  
Surface Glycoprotein ◽  
Major Surface Glycoprotein ◽  
Major Surface

scholarly journals Episomal Expression of Specific Sense and Antisense mRNAs in Leishmania amazonensis: Modulation of gp63 Level in Promastigotes and Their Infection of Macrophages In Vitro

2000 ◽  
Vol 68 (1) ◽  
pp. 80-86 ◽  
Author(s):  
De-Qiao Chen ◽  
Bala Krishna Kolli ◽  
Nagendra Yadava ◽  
Hong Gang Lu ◽  
Alice Gilman-Sachs ◽  
...  
Keyword(s):  
Kinetic Studies ◽  
Single Copy ◽  
Antisense Transcription ◽  
Leishmania Amazonensis ◽  
Surface Glycoprotein ◽  
Major Surface Glycoprotein ◽  
Wild Type Clone ◽  
Major Surface ◽  
Specific Sense

ABSTRACT The major surface glycoprotein (gp63) of Leishmania amazonensis is a metalloprotease implicated in the infection of mammalian macrophages. The expression of gp63 and its participation in this infection were further examined by modulating the level of this molecule in a virulent gp63-abundant wild-type clone. Promastigotes were transfected with gp63 genes cloned into aLeishmania-specific vector in two different orientations, leading to the expression of gp63 sense and antisense RNAs. With increasing selective pressure, cell surface gp63 was increasingly augmented in the transfectants with sense transcripts and suppressed to a very low level in those with antisense transcripts. Thus, the expression of gp63 from chromosomal, repetitive genes is not stringently regulated at the protein level and can be substantially reduced by episomal antisense transcription of a single copy. The transfectants differed significantly only in the level of gp63, thereby allowing specific evaluation of this molecule in leishmanial infection of macrophages in vitro. Kinetic studies of infection in vitro indicate that gp63 plays a role not only in the binding of this parasite to these macrophages but also in its intramacrophage survival and replication.

scholarly journals Partial Structure of Glutamic Acid and Alanine-rich Protein, a Major Surface Glycoprotein of the Insect Stages ofTrypanosoma congolense

2002 ◽  
Vol 277 (50) ◽  
pp. 48899-48904 ◽  
Author(s):  
Lynn M. Thomson ◽  
Douglas J. Lamont ◽  
Angela Mehlert ◽  
J. David Barry ◽  
Michael A. J. Ferguson
Keyword(s):  
Glutamic Acid ◽  
Protein A ◽  
Surface Glycoprotein ◽  
Partial Structure ◽  
Major Surface Glycoprotein ◽  
Major Surface

Involvement ofLeishmania donovani major surface glycoprotein gp63 in promastigote multiplication

2004 ◽  
Vol 29 (1) ◽  
pp. 15-22 ◽  
Author(s):  
Sanjeev Pandey ◽  
Phuljhuri Chakraborti ◽  
Rakhi Sharma ◽  
Santu Bandyopadhyay ◽  
Dwijen Sarkar ◽  
...  
Keyword(s):  
Surface Glycoprotein ◽  
Major Surface Glycoprotein ◽  
Major Surface

scholarly journals Defects in the N-Linked Oligosaccharide Biosynthetic Pathway in a Trypanosoma brucei Glycosylation Mutant

2004 ◽  
Vol 3 (2) ◽  
pp. 255-263 ◽  
Author(s):  
Alvaro Acosta-Serrano ◽  
Jessica O'Rear ◽  
George Quellhorst ◽  
Soo Hee Lee ◽  
Kuo-Yuan Hwa ◽  
...  
Keyword(s):  
Cell Line ◽  
Trypanosoma Brucei ◽  
Concanavalin A ◽  
Biosynthetic Pathway ◽  
Mutant Cell ◽  
Surface Glycoprotein ◽  
Wild Type ◽  
Mutant Cell Line ◽  
Major Surface Glycoprotein ◽  
Major Surface

ABSTRACT Concanavalin A (ConA) kills the procyclic (insect) form of Trypanosoma brucei by binding to its major surface glycoprotein, procyclin. We previously isolated a mutant cell line, ConA 1-1, that is less agglutinated and more resistant to ConA killing than are wild-type (WT) cells. Subsequently we found that the ConA resistance phenotype in this mutant is due to the fact that the procyclin either has no N-glycan or has an N-glycan with an altered structure. Here we demonstrate that the alteration in procyclin N-glycosylation correlates with two defects in the N-linked oligosaccharide biosynthetic pathway. First, ConA 1-1 has a defect in activity of polyprenol reductase, an enzyme involved in synthesis of dolichol. Metabolic incorporation of [3H]mevalonate showed that ConA 1-1 synthesizes equal amounts of dolichol and polyprenol, whereas WT cells make predominantly dolichol. Second, we found that ConA 1-1 synthesizes and accumulates an oligosaccharide lipid (OSL) precursor that is smaller in size than that from WT cells. The glycan of OSL in WT cells is apparently Man9GlcNAc2, whereas that from ConA 1-1 is Man7GlcNAc2. The smaller OSL glycan in the ConA 1-1 explains how some procyclin polypeptides bear a Man4GlcNAc2 modified with a terminal N-acetyllactosamine group, which is poorly recognized by ConA.

Sign in / Sign up

Export Citation Format

Share Document