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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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. |
doi_str_mv | 10.1016/S1383-5769(02)00015-6 |
format | Article |
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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
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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.</description><subject>Animals</subject><subject>Calcium</subject><subject>Extracellular matrix</subject><subject>Female</subject><subject>Fibronectin</subject><subject>Fibronectins - metabolism</subject><subject>Humans</subject><subject>Iron</subject><subject>Parasitism</subject><subject>Trichomonas vaginalis</subject><subject>Trichomonas vaginalis - metabolism</subject><subject>Trichomonas vaginalis - pathogenicity</subject><subject>Trichomonas Vaginitis - parasitology</subject><subject>Vagina - parasitology</subject><issn>1383-5769</issn><issn>1873-0329</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EoqXwCaCsECwCfsRxskKo4iVV6oKythxnQo0Su9htBTv-gT_kS3AfqEtWcxfnzmgOQqcEXxFM8utnwgqWcpGXF5heYowJT_M91CeFYClmtNyP-Q_poaMQ3laMEOQQ9QilGRMF7aPxZAqJdt2shY-kMZV3FvTc2J-v72TijZ66zlkVkqV6NVa1JiTGzsGryDgbEmXrHeaCCcfooFFtgJPtHKCX-7vJ8DEdjR-ehrejVGcZn6cC1zmIhte4YgwrLpiABjgveVnFXwpVKdBQCKxLnZGqyOpSV1VRUs1BxMQG6Hyzd-bd-wLCXHYmaGhbZcEtghSUkDzn9F-QFDkjZRQ1QHwDau9C8NDImTed8p-SYLlSLtfK5cqnxFSulcs89s62BxZVB_WutXUcgZsNANHH0oCXQRuwGmrjo2tZO_PPiV9Q_pL5</recordid><startdate>20020901</startdate><enddate>20020901</enddate><creator>Alderete, J.F</creator><creator>Benchimol, M</creator><creator>Lehker, M.W</creator><creator>Crouch, M.-L</creator><general>Elsevier Ireland Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>20020901</creationdate><title>The complex fibronectin– Trichomonas vaginalis interactions and Trichomonosis</title><author>Alderete, J.F ; Benchimol, M ; Lehker, M.W ; Crouch, M.-L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c445t-70d6e7f5d0b330a5737efe55959b0008abaece870c9c41b84d9cbb892c5e7cbb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Calcium</topic><topic>Extracellular matrix</topic><topic>Female</topic><topic>Fibronectin</topic><topic>Fibronectins - metabolism</topic><topic>Humans</topic><topic>Iron</topic><topic>Parasitism</topic><topic>Trichomonas vaginalis</topic><topic>Trichomonas vaginalis - metabolism</topic><topic>Trichomonas vaginalis - pathogenicity</topic><topic>Trichomonas Vaginitis - parasitology</topic><topic>Vagina - parasitology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alderete, J.F</creatorcontrib><creatorcontrib>Benchimol, M</creatorcontrib><creatorcontrib>Lehker, M.W</creatorcontrib><creatorcontrib>Crouch, M.-L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Parasitology International</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alderete, J.F</au><au>Benchimol, M</au><au>Lehker, M.W</au><au>Crouch, M.-L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The complex fibronectin– Trichomonas vaginalis interactions and Trichomonosis</atitle><jtitle>Parasitology International</jtitle><addtitle>Parasitol Int</addtitle><date>2002-09-01</date><risdate>2002</risdate><volume>51</volume><issue>3</issue><spage>285</spage><epage>292</epage><pages>285-292</pages><issn>1383-5769</issn><eissn>1873-0329</eissn><abstract>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
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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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