Two distinct hemolysins in Trichomonas tenax ATCC 30207

Abstract

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.

Detection of Oral Entamoeba Gingivalis and Trichomonas Tenax in Adult Quilombola Population with Periodontal Disease

“…However, the presence of these potentially pathogenic microorganisms in the oral cavity was more prevalent in the gingivitis condition when compared to periodontitis. It has been demonstrated that T. tenax presents activity mediated by cysteine endopeptidases which hydrolyze collagen molecules types I, III, IV, V and also lyse human eritrocytes (18)(19)(20).…”

Assessment of the role of Trichomonas tenax in the etiopathogenesis of human periodontitis: A systematic review

“…Authors have detected the capacity of T. tenax ATCC 30207 to adhere to diverse cells and induce cytotoxicity [17], while others studies showed no adherence or cytotoxic property [18][19]. Moreover, flagellates produce numerous enzymes, such as cysteine protease, cathepsin B like protein, haemolysins, metalloproteinase and other proteinases that could participate in the breakdown of collagen, gelatin observed in periodontal diseases [20][21][22][23][24][25]. Live trophozoites of the Hs-4 strain of T. tenax failed to induce secretion of IL-1β, IL-8, IL-10 or TNFα from macrophages.…”

“…But Bózner et al concluded that it would be of interest to purify T. tenax enzymes and test their effect on extracellular matrix proteins in the oral cavity [25]. In addition to these enzymes, T. tenax seems to be able to produce haemolysins, which are also synthesised by many pathobionts such as P. gingivalis, Prevotella intermedia, A. actinomycetemcomitans and Treponema denticola [50][51][52][53]22].…”

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

“…Nagao i wsp. stwierdzili, że hemolizyny syntetyzowane przez ten gatunek są zdolne do lizy erytrocytów ludzkich, owczych, króliczych i końskich (73). Enzymy wytwarzane przez T. tenax oddziaływają destrukcyjnie na błonę śluzową jamy ustnej i tkanki przyzębia (47,59,62).…”