The complex fibronectin– Trichomonas vaginalis interactions and Trichomonosis

Trichomonosis is the vaginitis caused by Trichomonas vaginalis. This sexually transmitted agent achieves successful host parasitism through various means including: (1) acquisition of nutrients through specific receptors; (2) recognition and binding to mucin followed by cytoadherence mediated by adh...

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Veröffentlicht in:Parasitology International 2002-09, Vol.51 (3), p.285-292
Hauptverfasser: Alderete, J.F, Benchimol, M, Lehker, M.W, Crouch, M.-L
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Benchimol, M
Lehker, M.W
Crouch, M.-L
description Trichomonosis is the vaginitis caused by Trichomonas vaginalis. This sexually transmitted agent achieves successful host parasitism through various means including: (1) acquisition of nutrients through specific receptors; (2) recognition and binding to mucin followed by cytoadherence mediated by adhesins that resemble metabolic enzymes; (3) evasion of immune responses through (i) masking of organisms by host proteins, (ii) shedding of trichomonad proteins into the secretions and (iii) secretions of cysteine proteinases that degrade all immunoglobulin subclasses and complement; (4) alternating surface expression of at least two antigen repertoires; and (5) alternate and coordinate expression of virulence genes in response to host environmental factors. The fact that the parasite survives long term in the varying and adverse environment of the vagina attests to the highly evolved nature of this protist. An understanding of the non-self-limiting nature of this infection may come from recent findings illustrating the complexity of Trichomonas vaginalis–fibronectin (FN) interactions. The parasite readily attaches to surfaces with immobilized FN and binds to FN in a highly specific receptor-mediated fashion. The amount and affinity of bound FN by live organisms is influenced by concentrations in medium of both iron and calcium. De novo protein synthesis is required for optimal FN acquisition in the presence of calcium. Furthermore, the parasites bind with differing affinities to the N-terminal domain (NTD), the cell-binding domain (CBD) and the gelatin-binding domain (GBD) of FN. Iron modulates binding of NTD similar to that of FN. This minireview summarizes recent findings on the T. vaginalis–FN associations.
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An understanding of the non-self-limiting nature of this infection may come from recent findings illustrating the complexity of Trichomonas vaginalis–fibronectin (FN) interactions. The parasite readily attaches to surfaces with immobilized FN and binds to FN in a highly specific receptor-mediated fashion. The amount and affinity of bound FN by live organisms is influenced by concentrations in medium of both iron and calcium. De novo protein synthesis is required for optimal FN acquisition in the presence of calcium. Furthermore, the parasites bind with differing affinities to the N-terminal domain (NTD), the cell-binding domain (CBD) and the gelatin-binding domain (GBD) of FN. Iron modulates binding of NTD similar to that of FN. 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subjects Animals
Calcium
Extracellular matrix
Female
Fibronectin
Fibronectins - metabolism
Humans
Iron
Parasitism
Trichomonas vaginalis
Trichomonas vaginalis - metabolism
Trichomonas vaginalis - pathogenicity
Trichomonas Vaginitis - parasitology
Vagina - parasitology
title The complex fibronectin– Trichomonas vaginalis interactions and Trichomonosis
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