The pathobiology ofTrichomonas vaginalisinvolves direct and indirect interactions with host tissue, bacteria and viruses. In this work, we investigated adhesion and interaction with human microbiota, pathogenic mechanisms of protozoan.We characterized a new protein, TVAG339720, belonging to M60-like/PF13402 domain-containing proteins. M60-like domains are shared by proteins from several mucosal microbes, hypothetically relating with epithelial cells. TVAG339720 is characterized by a signal peptide, a transmembran domain, and putative carbohydrate binding modules, PA14 and GBDL, supposed to bind to heparin and heparan sulphate (HS). HS are sugars forming proteoglycans, a component of epithelial cells glycocalyx. We tested protease activity of TVAG339720 towards proteoglycans and interaction between CBMs, heparin and HS. Although the target of TVAG339720-M60L is still unknown, the bounds between TVAG339720-CBMs and HS suggest that these proteases play a role in adhesion to epithelial layer.T.vaginalisinteractions with microbes of urogenital tract represent another pathogenic mechanism. We focused on symbiosis established withMycoplasma hominis, studying howM.hominisinfluencesT.vaginalispathobiologyin vitro. Comparing the ATP produced by free-protozoan andT.vaginaliswithM.hominisand evaluating mycoplasma ability to influence nitric oxide production by macrophage inT. vaginalisinfections, we can assert that this is a mutually beneficial endosymbiotic relationship.

Several aspects of pathogenesis ofTrichomonas vaginalis / Margarita, Valentina. - (2015 Feb 27).

Several aspects of pathogenesis ofTrichomonas vaginalis

MARGARITA, Valentina
2015-02-27

Abstract

The pathobiology ofTrichomonas vaginalisinvolves direct and indirect interactions with host tissue, bacteria and viruses. In this work, we investigated adhesion and interaction with human microbiota, pathogenic mechanisms of protozoan.We characterized a new protein, TVAG339720, belonging to M60-like/PF13402 domain-containing proteins. M60-like domains are shared by proteins from several mucosal microbes, hypothetically relating with epithelial cells. TVAG339720 is characterized by a signal peptide, a transmembran domain, and putative carbohydrate binding modules, PA14 and GBDL, supposed to bind to heparin and heparan sulphate (HS). HS are sugars forming proteoglycans, a component of epithelial cells glycocalyx. We tested protease activity of TVAG339720 towards proteoglycans and interaction between CBMs, heparin and HS. Although the target of TVAG339720-M60L is still unknown, the bounds between TVAG339720-CBMs and HS suggest that these proteases play a role in adhesion to epithelial layer.T.vaginalisinteractions with microbes of urogenital tract represent another pathogenic mechanism. We focused on symbiosis established withMycoplasma hominis, studying howM.hominisinfluencesT.vaginalispathobiologyin vitro. Comparing the ATP produced by free-protozoan andT.vaginaliswithM.hominisand evaluating mycoplasma ability to influence nitric oxide production by macrophage inT. vaginalisinfections, we can assert that this is a mutually beneficial endosymbiotic relationship.
Trichomonas vaginalis; pathogenesis; adhesion; M60-like domain-containing proteins; Mycoplasma hominis
Several aspects of pathogenesis ofTrichomonas vaginalis / Margarita, Valentina. - (2015 Feb 27).
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11388/250469
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