Cloning and characterization of glycogen branching and debranching enzymes from the parasitic protist Trichomonas vaginalis

Biochimie ◽  
2021 ◽  
Vol 186 ◽  
pp. 59-72
Author(s):  
Karoline E. Dittmer ◽  
Prajakta Pradhan ◽  
Quentin C. Tompkins ◽  
Andrew Brittingham ◽  
Wayne A. Wilson
Keyword(s):  
Trichomonas Vaginalis ◽  
Debranching Enzymes ◽  
Parasitic Protist

scholarly journals Expression and characterization of a β-fructofuranosidase from the parasitic protist Trichomonas vaginalis

2014 ◽  
Vol 15 (1) ◽  
pp. 12 ◽  
Author(s):  
Michael Dirkx ◽  
Michael P Boyer ◽  
Prajakta Pradhan ◽  
Andrew Brittingham ◽  
Wayne A Wilson
Keyword(s):  
Trichomonas Vaginalis ◽  
Parasitic Protist

Structural characterization of novel inositol phosphosphingolipids of Tritrichomonas foetus and Trichomonas vaginalis

Glycobiology ◽  
1993 ◽  
Vol 3 (3) ◽  
pp. 261-269 ◽  
Author(s):  
Catherine E. Costello ◽  
John Glushka ◽  
Herman van Halbeek ◽  
Bibhuti N. Singh
Keyword(s):  
Structural Characterization ◽  
Trichomonas Vaginalis ◽  
Tritrichomonas Foetus

P86 Characterization of the ribosome from an amitochondriate protist, Trichomonas vaginalis

2001 ◽  
Vol 52 (Supplement) ◽  
pp. 99
Author(s):  
Nobuko ARISUE ◽  
Yasushi MAKI ◽  
Hideji YOSHIDA ◽  
Akira WADA ◽  
Tetsuo HASHIMOTO
Keyword(s):  
Trichomonas Vaginalis

scholarly journals BspA and Pmp proteins ofTrichomonas vaginalismediate adherence to host cells

2018 ◽  
Author(s):  
Maria R. Handrich ◽  
Sriram G. Garg ◽  
Ewen W. Sommerville ◽  
Robert P. Hirt ◽  
Sven B. Gould
Keyword(s):  
Trichomonas Vaginalis ◽  
Functional Characterization ◽  
Surface Proteins ◽  
Host Cells ◽  
Protein Families ◽  
Sexually Transmitted ◽  
Trace Back ◽  
Oral Pathogens ◽  
Adhesion Performance

AbstractTrichomonas vaginalisis one of the most widespread, sexually transmitted pathogens. The infection involves a morphological switch from a free-swimming pyriform trophozoite to an amoeboid cell upon adhesion to host epithelial cells. While details on how the switch is induced and to what proteins of the host surface the parasite adheres remain poorly characterized, several surface proteins of the parasite itself have been identified as potential candidates. Among those are two expanded protein families that harbor domains that share similarity to functionally investigated surface proteins of prokaryotic oral pathogens; these are the BspA proteins of Bacteroidales and Spirochaetales, and the Pmp proteins of Chlamydiales. We sequenced the transcriptomes of five Trichomonads and screened for the presence of BspA and Pmp domain-containing proteins and tested the ability of individualT. vaginaliscandidates to mediate adhesion. Here we demonstrate that (i) BspA and Pmp domain-containing proteins are specifically expanded inT. vaginalisin comparison to other Trichomonads, and that (ii) individual proteins of both families have the ability to increase adhesion performance in a non-virulentT. vaginalisstrain andTetratrichomonas gallinarum, a parasite usually known to infect birds but not humans. Our results initiate the functional characterization of these two broadly distributed protein families, whose origin we trace back to the origin of Trichomonads themselves.

scholarly journals Purification and characterization of methionine γ-lyase from Trichomonas vaginalis

1991 ◽  
Vol 279 (3) ◽  
pp. 675-682 ◽  
Author(s):  
B C Lockwood ◽  
G H Coombs
Keyword(s):  
Molecular Mass ◽  
Trichomonas Vaginalis ◽  
Protozoan Parasite ◽  
Purification And Characterization ◽  
Native Molecular Mass ◽  
Substrate Analogues ◽  
Beta Elimination ◽  
Derivatives Of ◽  
Methionine Gamma Lyase

Methionine gamma-lyase (EC 4.4.1.11) was purified to homogeneity from the anaerobic protozoan parasite Trichomonas vaginalis by a series of f.p.l.c. procedures. The enzyme catalyses alpha gamma- and alpha beta-elimination reactions of a number of derivatives of methionine and cysteine. It also catalyses gamma-replacement reactions of the thiomethyl group of methionine, homocysteine and ethionine to yield the corresponding S-substituted homocysteine derivative. The enzyme is pyridoxal 5′-phosphate-dependent, has a native molecular mass of approx. 160 kDa and consists of four apparently identical subunits of molecular mass 43-45 kDa. The absorption spectrum of the enzyme is typical of those obtained for other pyridoxal 5′-phosphate-dependent enzymes, and the holoenzyme can be resolved to the apoenzyme by incubation with hydroxylamine and reconstituted by addition of the cofactor. The enzyme activity is significantly affected by carbonyl and thiol reagents, is competitively inhibited by a number of substrate analogues and is completely inactivated by the suicide inhibitor DL-propargylglycine. The T. vaginalis enzyme is similar, in terms of activity and properties, to the enzymes found in a number of species of bacteria that metabolize methionine under anaerobic conditions. It is suggested that methionine catabolism may be of particular importance to the survival of T. vaginalis under microaerophilic conditions in its host.

scholarly journals Purification and characterization of pyruvate: ferredoxin oxidoreductase from the anaerobic protozoon Trichomonas vaginalis

1987 ◽  
Vol 246 (2) ◽  
pp. 529-536 ◽  
Author(s):  
K Williams ◽  
P N Lowe ◽  
P F Leadlay
Keyword(s):  
Trichomonas Vaginalis ◽  
Salting Out ◽  
Iron Protein ◽  
Ferredoxin Oxidoreductase ◽  
Membrane Bound ◽  
Pyruvate Ferredoxin Oxidoreductase ◽  
Bacterial Sources ◽  
Sepharose 4B ◽  
Thiamin Pyrophosphate

The pyruvate: ferredoxin oxidoreductase from the anaerobic protozoon Trichomonas vaginalis is an extrinsic protein bound to the hydrogenosomal membrane. It has been solubilized and purified to homogeneity, principally by salting-out chromatography on Sepharose 4B. Low recoveries of active enzyme were caused by inactivation by O2 and the irreversible loss of thiamin pyrophosphate. It is a dimeric enzyme of overall Mr 240,000 and subunit Mr 120,000. The enzyme contains, per mol of dimer, 7.3 +/- 0.3 mol of iron and 5.9 +/- 0.9 mol of acid-labile sulphur, suggesting the presence of two [4Fe-4S] centres, and 0.47 mol of thiamin pyrophosphate. The absorption spectrum of the enzyme is characteristic of a non-haem iron protein. The pyruvate: ferredoxin oxidoreductase from T. vaginalis is therefore broadly similar to the 2-oxo acid: ferredoxin (flavodoxin) oxidoreductases purified from bacterial sources, except that it is membrane-bound.

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