Cell-associated and extracellular proteolytic activity of an oral flagellate, Trichomonas tenax

Bozner, Peter; Demĕs, P

doi:10.1016/0003-9969(91)90056-z

Cited by 19 publications

(25 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A correlation between the presence of T. tenax and tissue changes in the oral cavity has not been found (Hayawan and Bayoumy 1992). However, this protozoan has been shown to possess a number of proteinases; these include proteinase with collagenolytic activity (Bózner and Demes 1991b) and other cysteine proteinases (Bózner and Demes 1991a).…”

Section: Introductionmentioning

confidence: 99%

Phylogenetic Position of the Mitochondrion-Lacking Protozoan Trichomonas tenax, Based on Amino Acid Sequences of Elongation Factors 1α and 2

et al. 1997

View full text Add to dashboard Cite

Major parts of amino-acid-coding regions of elongation factor (EF)-1alpha and EF-2 in Trichomonas tenax were amplified by PCR from total genomic DNA and the products were cloned into a plasmid vector, pGEM-T. The three clones from each of the products of the EF-1alpha and EF-2 were isolated and sequenced. The insert DNAs of the clones containing EF-1alpha coding regions were each 1,185 bp long with the same nucleotide sequence and contained 53.1% of G + C nucleotides. Those of the clones containing EF-2 coding regions had two different sequences; one was 2,283 bp long and the other was 2,286 bp long, and their G + C contents were 52.5 and 52.9%, respectively. The copy numbers of the EF-1alpha and EF-2 gene per chromosome were estimated as four and two, respectively. The deduced amino acid sequences obtained by the conceptual translation were 395 residues from EF-1alpha and 761 and 762 residues from the EF-2s. The sequences were aligned with the other eukaryotic and archaebacterial EF-1alphas and EF-2s, respectively. The phylogenetic position of T. tenax was inferred by the maximum likelihood (ML) method using the EF-1alpha and EF-2 data sets. The EF-1alpha analysis suggested that three mitochondrion-lacking protozoa, Glugea plecoglossi, Giardia lamblia, and T. tenax, respectively, diverge in this order in the very early phase of eukaryotic evolution. The EF-2 analysis also supported the divergence of T. tenax to be immediately next to G. lamblia.

show abstract

Section: Introductionmentioning

confidence: 99%

Phylogenetic Position of the Mitochondrion-Lacking Protozoan Trichomonas tenax, Based on Amino Acid Sequences of Elongation Factors 1α and 2

et al. 1997

View full text Add to dashboard Cite

show abstract

“…T. tenax cell suspension (2×10 8 cells/ml in PBS) was incubated at 37°C for 6 h to infuse cellular products and centrifuged for 15 min at 700× g at 4°C and the supernatant passed through a 0.2‐μm membrane filter (Millipore Corp.). The resulting culture filtrate was monitored for the contamination of cells as the culture supernatant and was prepared as culture filtrate according to Bózner et al ( 3). The pellet was resuspended in the initial volume of PBS and used as the cell debris.…”

Section: Methodsmentioning

confidence: 99%

“…Trichomonas tenax is a mitochondrion‐lacking protist that is classified in the same genus as Trichomonas vaginalis and supposed to have diverged at very early phase of eukaryotic evolution ( 10, 30). It inhabits the human oral cavity and is more frequently found in persons with poor oral hygiene and in those with advanced periodontal diseases ( 3, 11, 18). T. tenax has also been isolated from infected submaxillar glands ( 8), pleural fluid of respiratory trichomoniasis ( 23) or bronchoalveolar fluid of pulmonary eosinophilia ( 17).…”

mentioning

confidence: 99%

Two distinct hemolysins in Trichomonas tenax ATCC 30207

Nagao¹,

Yamamoto

Igarashi

et al. 2000

Oral Microbiology and Immunology

View full text Add to dashboard Cite

An oral protist Trichomonas tenax ATCC 30207 was investigated for the ability to lyse erythrocytes of sheep, rabbits, horses and humans. Five fractions, including intact cells, culture supernatant, culture filtrate, cell debris and lipid-enriched fractions, were prepared from the protozoan cells, and their hemolytic activities were assayed under various conditions. All the samples except culture supernatant had hemolytic activities, which were due to two different kinds of hemolysins. One hemolysin was protein-like and mainly found in cell-free fractions: culture supernatant and culture filtrate. It was heat-labile and inhibited by various cysteine-proteinase inhibitors. The other hemolysin was lipid-like and found in cell-associated fractions: intact cells, cell-debris and lipid-enriched fractions. It was heat-stable, organic solvent-tolerant and unaffected by various proteinase inhibitors and stimulators. These results suggested that T. tenax ATCC 30207 possessed two distinct hemolysins, protein and lipid.

show abstract

“…Występowanie znacznej aktywności proteolitycznej stwierdzono także w przypadku T. tenax. Badania dowiodły, że gatunek ten wytwarza liczne proteazy, w tym metaloproteinazy, proteinazy cysteinowe i katepsyny odpowiedzialne za depolimeryzację włókien kolagenowych i degradację proteoglikanów (14,15,84,97). Dodatkowo T. tenax produkuje toksyny o działaniu cytotoksycznym.…”

Section: Chorobotwórczość I Czynniki Zjadliwościunclassified

Systematics, biology and invasiology of trichomonads (Trichomonadida) - the current state of knowledge

Szczepaniak¹,

Tomczuk²,

Łojszczyk-Szczepaniak³

et al. 2017

Medycyna Weterynaryjna

View full text Add to dashboard Cite

Trichomonads are anaerobic, flagellated protists belonging to the large phylum Parabasalia. In most cases, they exist as endosymbionts – harmless comensals of invertebrates and vertebrates – but several species are considered to be imported intestinal or urogenital parasites of humans and other animals. This paper presents current information on the taxonomy, morphology and biology of trichomonads. The characterization of invasiology followed by the description of virulence factors and pathogenic mechanisms of trichomonads is presented. The present paper also reviews diagnostic methods, treatment and prevention of trichomoniasis.

show abstract

Cell-associated and extracellular proteolytic activity of an oral flagellate, Trichomonas tenax

Cited by 19 publications

References 19 publications

Phylogenetic Position of the Mitochondrion-Lacking Protozoan Trichomonas tenax, Based on Amino Acid Sequences of Elongation Factors 1α and 2

Phylogenetic Position of the Mitochondrion-Lacking Protozoan Trichomonas tenax, Based on Amino Acid Sequences of Elongation Factors 1α and 2

Two distinct hemolysins in Trichomonas tenax ATCC 30207

Systematics, biology and invasiology of trichomonads (Trichomonadida) - the current state of knowledge

Contact Info

Product

Resources

About