Role of Carbohydrate-mediated Adherence in Cytopathogenic Mechanisms of Acanthamoeba
Acanthamoeba keratitis is a vision-threatening corneal infection. The mannose-binding protein of Acanthamoeba is thought to mediate adhesion of parasites to host cells. We characterized the amoeba lectin with respect to its carbohydrate binding properties and the role in amoeba-induced cytopathic ef...
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| Veröffentlicht in: | The Journal of biological chemistry 1998-06, Vol.273 (25), p.15838-15845 |
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| creator | Cao, Z Jefferson, D M Panjwani, N |
| description | Acanthamoeba keratitis is a vision-threatening corneal infection. The mannose-binding protein of Acanthamoeba is thought to mediate adhesion of parasites to host cells. We characterized the amoeba lectin with respect to its carbohydrate
binding properties and the role in amoeba-induced cytopathic effect (CPE). Sugar inhibition assays revealed that the amoeba
lectin has the highest affinity for α-Man and Man(α1â3)Man units. In vitro cytopathic assays indicated that mannose-based saccharides which inhibit amoeba adhesion to corneal epithelial cells were
also potent inhibitors of amoeba-induced CPE. Another major finding was that N -acetyl- d -glucosamine (GlcNAc) which does not inhibit adhesion of amoeba to host cells is also an inhibitor of amoeba-induced CPE.
The Acanthamoebae are thought to produce CPE by secreting cytotoxic proteinases. By zymography, one metalloproteinase and three serine proteinases
were detected in the conditioned media obtained after incubating amoebae with the host cells. The addition of free α-Man and
GlcNAc to the co-culture media inhibited the secretion of the metalloproteinase and serine proteinases, respectively. In summary,
we have shown that the lectin-mediated adhesion of the Acanthamoeba to host cells is a prerequisite for the amoeba-induced cytolysis of target cells and have implicated a contact-dependent
metalloproteinase in the cytopathogenic mechanisms of Acanthamoeba . |
| doi_str_mv | 10.1074/jbc.273.25.15838 |
| format | Article |
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binding properties and the role in amoeba-induced cytopathic effect (CPE). Sugar inhibition assays revealed that the amoeba
lectin has the highest affinity for α-Man and Man(α1â3)Man units. In vitro cytopathic assays indicated that mannose-based saccharides which inhibit amoeba adhesion to corneal epithelial cells were
also potent inhibitors of amoeba-induced CPE. Another major finding was that N -acetyl- d -glucosamine (GlcNAc) which does not inhibit adhesion of amoeba to host cells is also an inhibitor of amoeba-induced CPE.
The Acanthamoebae are thought to produce CPE by secreting cytotoxic proteinases. By zymography, one metalloproteinase and three serine proteinases
were detected in the conditioned media obtained after incubating amoebae with the host cells. The addition of free α-Man and
GlcNAc to the co-culture media inhibited the secretion of the metalloproteinase and serine proteinases, respectively. In summary,
we have shown that the lectin-mediated adhesion of the Acanthamoeba to host cells is a prerequisite for the amoeba-induced cytolysis of target cells and have implicated a contact-dependent
metalloproteinase in the cytopathogenic mechanisms of Acanthamoeba .</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.273.25.15838</identifier><identifier>PMID: 9624184</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Acanthamoeba ; Acanthamoeba - pathogenicity ; Acanthamoeba Keratitis - parasitology ; Acanthamoeba Keratitis - pathology ; Acute-Phase Proteins - metabolism ; Animals ; Carrier Proteins - metabolism ; Cell Adhesion - drug effects ; Freshwater ; Humans ; Lectins - metabolism ; Mannans - metabolism ; Mannose - metabolism ; Mannose-Binding Lectins ; Rabbits ; Serine Proteinase Inhibitors - pharmacology</subject><ispartof>The Journal of biological chemistry, 1998-06, Vol.273 (25), p.15838-15845</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c398t-f96645717b9b515fbf40177ab849c2f0c11603d3f0c64a759679d9e82e885fe83</citedby><cites>FETCH-LOGICAL-c398t-f96645717b9b515fbf40177ab849c2f0c11603d3f0c64a759679d9e82e885fe83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9624184$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cao, Z</creatorcontrib><creatorcontrib>Jefferson, D M</creatorcontrib><creatorcontrib>Panjwani, N</creatorcontrib><title>Role of Carbohydrate-mediated Adherence in Cytopathogenic Mechanisms of Acanthamoeba</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Acanthamoeba keratitis is a vision-threatening corneal infection. The mannose-binding protein of Acanthamoeba is thought to mediate adhesion of parasites to host cells. We characterized the amoeba lectin with respect to its carbohydrate
binding properties and the role in amoeba-induced cytopathic effect (CPE). Sugar inhibition assays revealed that the amoeba
lectin has the highest affinity for α-Man and Man(α1â3)Man units. In vitro cytopathic assays indicated that mannose-based saccharides which inhibit amoeba adhesion to corneal epithelial cells were
also potent inhibitors of amoeba-induced CPE. Another major finding was that N -acetyl- d -glucosamine (GlcNAc) which does not inhibit adhesion of amoeba to host cells is also an inhibitor of amoeba-induced CPE.
The Acanthamoebae are thought to produce CPE by secreting cytotoxic proteinases. By zymography, one metalloproteinase and three serine proteinases
were detected in the conditioned media obtained after incubating amoebae with the host cells. The addition of free α-Man and
GlcNAc to the co-culture media inhibited the secretion of the metalloproteinase and serine proteinases, respectively. In summary,
we have shown that the lectin-mediated adhesion of the Acanthamoeba to host cells is a prerequisite for the amoeba-induced cytolysis of target cells and have implicated a contact-dependent
metalloproteinase in the cytopathogenic mechanisms of Acanthamoeba .</description><subject>Acanthamoeba</subject><subject>Acanthamoeba - pathogenicity</subject><subject>Acanthamoeba Keratitis - parasitology</subject><subject>Acanthamoeba Keratitis - pathology</subject><subject>Acute-Phase Proteins - metabolism</subject><subject>Animals</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Adhesion - drug effects</subject><subject>Freshwater</subject><subject>Humans</subject><subject>Lectins - metabolism</subject><subject>Mannans - metabolism</subject><subject>Mannose - metabolism</subject><subject>Mannose-Binding Lectins</subject><subject>Rabbits</subject><subject>Serine Proteinase Inhibitors - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLxDAUhYMoOj72boQuxF3HpEmaZDkMvkARRMFdSNJbG5k2Y9JB5t8bnUFw5d2cC-ex-BA6JXhKsGCX79ZNK0GnFZ8SLqncQROCJS0pJ6-7aIJxRUpVcXmADlN6x_mYIvtoX9UVI5JN0PNTWEAR2mJuog3duolmhLKHxmdtilnTQYTBQeGHYr4ew9KMXXiDwbviAVxnBp_69N2fOTOMnekDWHOM9lqzSHCy1SP0cn31PL8t7x9v7uaz-9JRJceyVXXNuCDCKssJb23LMBHCWMmUq1rsCKkxbWj-amYEV7VQjQJZgZS8BUmP0MVmdxnDxwrSqHufHCwWZoCwSlooRSnj_N8gqTmTNRU5iDdBF0NKEVq9jL43ca0J1t_EdSauM3Fdcf1DPFfOttsrm7n9FraIs3--8Tv_1n36CNr64Dro_858ASl2h7c</recordid><startdate>19980619</startdate><enddate>19980619</enddate><creator>Cao, Z</creator><creator>Jefferson, D M</creator><creator>Panjwani, N</creator><general>American Society for Biochemistry and Molecular Biology</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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>19980619</creationdate><title>Role of Carbohydrate-mediated Adherence in Cytopathogenic Mechanisms of Acanthamoeba</title><author>Cao, Z ; Jefferson, D M ; Panjwani, N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c398t-f96645717b9b515fbf40177ab849c2f0c11603d3f0c64a759679d9e82e885fe83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Acanthamoeba</topic><topic>Acanthamoeba - pathogenicity</topic><topic>Acanthamoeba Keratitis - parasitology</topic><topic>Acanthamoeba Keratitis - pathology</topic><topic>Acute-Phase Proteins - metabolism</topic><topic>Animals</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Adhesion - drug effects</topic><topic>Freshwater</topic><topic>Humans</topic><topic>Lectins - metabolism</topic><topic>Mannans - metabolism</topic><topic>Mannose - metabolism</topic><topic>Mannose-Binding Lectins</topic><topic>Rabbits</topic><topic>Serine Proteinase Inhibitors - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cao, Z</creatorcontrib><creatorcontrib>Jefferson, D M</creatorcontrib><creatorcontrib>Panjwani, N</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cao, Z</au><au>Jefferson, D M</au><au>Panjwani, N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of Carbohydrate-mediated Adherence in Cytopathogenic Mechanisms of Acanthamoeba</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1998-06-19</date><risdate>1998</risdate><volume>273</volume><issue>25</issue><spage>15838</spage><epage>15845</epage><pages>15838-15845</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Acanthamoeba keratitis is a vision-threatening corneal infection. The mannose-binding protein of Acanthamoeba is thought to mediate adhesion of parasites to host cells. We characterized the amoeba lectin with respect to its carbohydrate
binding properties and the role in amoeba-induced cytopathic effect (CPE). Sugar inhibition assays revealed that the amoeba
lectin has the highest affinity for α-Man and Man(α1â3)Man units. In vitro cytopathic assays indicated that mannose-based saccharides which inhibit amoeba adhesion to corneal epithelial cells were
also potent inhibitors of amoeba-induced CPE. Another major finding was that N -acetyl- d -glucosamine (GlcNAc) which does not inhibit adhesion of amoeba to host cells is also an inhibitor of amoeba-induced CPE.
The Acanthamoebae are thought to produce CPE by secreting cytotoxic proteinases. By zymography, one metalloproteinase and three serine proteinases
were detected in the conditioned media obtained after incubating amoebae with the host cells. The addition of free α-Man and
GlcNAc to the co-culture media inhibited the secretion of the metalloproteinase and serine proteinases, respectively. In summary,
we have shown that the lectin-mediated adhesion of the Acanthamoeba to host cells is a prerequisite for the amoeba-induced cytolysis of target cells and have implicated a contact-dependent
metalloproteinase in the cytopathogenic mechanisms of Acanthamoeba .</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9624184</pmid><doi>10.1074/jbc.273.25.15838</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79933455 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acanthamoeba Acanthamoeba - pathogenicity Acanthamoeba Keratitis - parasitology Acanthamoeba Keratitis - pathology Acute-Phase Proteins - metabolism Animals Carrier Proteins - metabolism Cell Adhesion - drug effects Freshwater Humans Lectins - metabolism Mannans - metabolism Mannose - metabolism Mannose-Binding Lectins Rabbits Serine Proteinase Inhibitors - pharmacology |
| title | Role of Carbohydrate-mediated Adherence in Cytopathogenic Mechanisms of Acanthamoeba |
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