Degradation of Human IgA by Entamoeba histolytica
To determine whether the virulent enteric pathogen Entamoeba histolytica degrades human IgA molecules, serum and secretory IgA was exposed to viable axenic trophozoites (strain HM1:IMSS), a parasite sonicate, and medium conditioned by incubation with live trophozoites. IgA was completely degraded un...
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| Veröffentlicht in: | The Journal of infectious diseases 1993-11, Vol.168 (5), p.1319-1322 |
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| container_title | The Journal of infectious diseases |
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| creator | Kelsall, Brian L. Ravdin, Jonathan I. |
| description | To determine whether the virulent enteric pathogen Entamoeba histolytica degrades human IgA molecules, serum and secretory IgA was exposed to viable axenic trophozoites (strain HM1:IMSS), a parasite sonicate, and medium conditioned by incubation with live trophozoites. IgA was completely degraded under all conditions, proteinase activity was maximal at a neutral pH, and there was a four- to eightfold enrichment of amebic IgA proteolytic activity in a soluble fraction of amebic sonicate. Degradation of serum IgA by amebic sonicate was completely inhibited by the cysteine proteinase inhibitors trans-epoxysuccinyl-l-Ieucylamino(4-guanidino)butane (E-64, 100 µ,M) and benzyloxycarbonyl-phenyl-alanyl-alanyl-fluoromethyl ketone (Z-Phe-AlaCH2F, 12.5 µM). Secretion of degradative activity, the optimal pH, and the inhibition by E-64 and Z-Phe-Ala-CH2F indicates that cysteine proteinase activity is predominately responsible for the degradation of human IgA by E. histolytica. |
| doi_str_mv | 10.1093/infdis/168.5.1319 |
| format | Article |
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IgA was completely degraded under all conditions, proteinase activity was maximal at a neutral pH, and there was a four- to eightfold enrichment of amebic IgA proteolytic activity in a soluble fraction of amebic sonicate. Degradation of serum IgA by amebic sonicate was completely inhibited by the cysteine proteinase inhibitors trans-epoxysuccinyl-l-Ieucylamino(4-guanidino)butane (E-64, 100 µ,M) and benzyloxycarbonyl-phenyl-alanyl-alanyl-fluoromethyl ketone (Z-Phe-AlaCH2F, 12.5 µM). Secretion of degradative activity, the optimal pH, and the inhibition by E-64 and Z-Phe-Ala-CH2F indicates that cysteine proteinase activity is predominately responsible for the degradation of human IgA by E. histolytica.</description><identifier>ISSN: 0022-1899</identifier><identifier>EISSN: 1537-6613</identifier><identifier>DOI: 10.1093/infdis/168.5.1319</identifier><identifier>PMID: 8228372</identifier><identifier>CODEN: JIDIAQ</identifier><language>eng</language><publisher>Chicago, IL: The University of Chicago Press</publisher><subject>Animals ; Biological and medical sciences ; Concise Communications ; Cysteine Endopeptidases - metabolism ; Cysteine Proteinase Inhibitors - pharmacology ; Dipeptides - pharmacology ; Entamoeba histolytica ; Entamoeba histolytica - enzymology ; Entamoeba histolytica - metabolism ; Enzymes ; Epithelial cells ; Fundamental and applied biological sciences. Psychology ; Humans ; Immunoglobulin A - metabolism ; Immunoglobulins ; Infectious diseases ; Ketones - pharmacology ; Leucine - analogs & derivatives ; Leucine - pharmacology ; Life cycle. Host-agent relationship. Pathogenesis ; Mucus ; Parasites ; Particulate matter ; Protease inhibitors ; Protozoa ; Secretion ; Subcellular Fractions - enzymology ; Subcellular Fractions - metabolism ; Trophozoites</subject><ispartof>The Journal of infectious diseases, 1993-11, Vol.168 (5), p.1319-1322</ispartof><rights>Copyright 1993 The University of Chicago</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-e34d52eb9424cf0866556201933a323dbfb5cd82e892b00c10d625655956374e3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30113659$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30113659$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4070200$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8228372$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kelsall, Brian L.</creatorcontrib><creatorcontrib>Ravdin, Jonathan I.</creatorcontrib><title>Degradation of Human IgA by Entamoeba histolytica</title><title>The Journal of infectious diseases</title><addtitle>J Infect Dis</addtitle><description>To determine whether the virulent enteric pathogen Entamoeba histolytica degrades human IgA molecules, serum and secretory IgA was exposed to viable axenic trophozoites (strain HM1:IMSS), a parasite sonicate, and medium conditioned by incubation with live trophozoites. IgA was completely degraded under all conditions, proteinase activity was maximal at a neutral pH, and there was a four- to eightfold enrichment of amebic IgA proteolytic activity in a soluble fraction of amebic sonicate. Degradation of serum IgA by amebic sonicate was completely inhibited by the cysteine proteinase inhibitors trans-epoxysuccinyl-l-Ieucylamino(4-guanidino)butane (E-64, 100 µ,M) and benzyloxycarbonyl-phenyl-alanyl-alanyl-fluoromethyl ketone (Z-Phe-AlaCH2F, 12.5 µM). Secretion of degradative activity, the optimal pH, and the inhibition by E-64 and Z-Phe-Ala-CH2F indicates that cysteine proteinase activity is predominately responsible for the degradation of human IgA by E. histolytica.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Concise Communications</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Dipeptides - pharmacology</subject><subject>Entamoeba histolytica</subject><subject>Entamoeba histolytica - enzymology</subject><subject>Entamoeba histolytica - metabolism</subject><subject>Enzymes</subject><subject>Epithelial cells</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Immunoglobulin A - metabolism</subject><subject>Immunoglobulins</subject><subject>Infectious diseases</subject><subject>Ketones - pharmacology</subject><subject>Leucine - analogs & derivatives</subject><subject>Leucine - pharmacology</subject><subject>Life cycle. Host-agent relationship. Pathogenesis</subject><subject>Mucus</subject><subject>Parasites</subject><subject>Particulate matter</subject><subject>Protease inhibitors</subject><subject>Protozoa</subject><subject>Secretion</subject><subject>Subcellular Fractions - enzymology</subject><subject>Subcellular Fractions - metabolism</subject><subject>Trophozoites</subject><issn>0022-1899</issn><issn>1537-6613</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkDtPwzAUhS0EKuXxAxiQMiC2tNe-sZ2MqBRagcRSVMRiOY5TAnmAnUr035OopYxMd_jOOVf6CLmgMKKQ4Lio86zwYyriER9RpMkBGVKOMhSC4iEZAjAW0jhJjsmJ9-8AEKGQAzKIGYtRsiGht3bldKbboqmDJg9m60rXwXx1E6SbYFq3umpsqoO3wrdNuWkLo8_IUa5Lb89395Q8300Xk1n4-HQ_n9w8hiaKWRtajDLObJpELDI5xEJwLhjQBFEjwyzNU26ymNk4YSmAoZAJxrtQwgXKyOIpud7ufrrma219q6rCG1uWurbN2ispgCMw_DfY2WGcyz5It0HjGu-dzdWnKyrtNoqC6n2qrc--objqfXady934Oq1stm_sBHb8ase1N7rMna5Nt_Abi0ACA_ibee88uj1GoBQF79-EW955tt97rt2HEhIlV7OXVzVbLieSPixUhD--mJSz</recordid><startdate>19931101</startdate><enddate>19931101</enddate><creator>Kelsall, Brian L.</creator><creator>Ravdin, Jonathan I.</creator><general>The University of Chicago Press</general><general>University of Chicago Press</general><scope>BSCLL</scope><scope>IQODW</scope><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>19931101</creationdate><title>Degradation of Human IgA by Entamoeba histolytica</title><author>Kelsall, Brian L. ; Ravdin, Jonathan I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-e34d52eb9424cf0866556201933a323dbfb5cd82e892b00c10d625655956374e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Concise Communications</topic><topic>Cysteine Endopeptidases - metabolism</topic><topic>Cysteine Proteinase Inhibitors - pharmacology</topic><topic>Dipeptides - pharmacology</topic><topic>Entamoeba histolytica</topic><topic>Entamoeba histolytica - enzymology</topic><topic>Entamoeba histolytica - metabolism</topic><topic>Enzymes</topic><topic>Epithelial cells</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Immunoglobulin A - metabolism</topic><topic>Immunoglobulins</topic><topic>Infectious diseases</topic><topic>Ketones - pharmacology</topic><topic>Leucine - analogs & derivatives</topic><topic>Leucine - pharmacology</topic><topic>Life cycle. Host-agent relationship. Pathogenesis</topic><topic>Mucus</topic><topic>Parasites</topic><topic>Particulate matter</topic><topic>Protease inhibitors</topic><topic>Protozoa</topic><topic>Secretion</topic><topic>Subcellular Fractions - enzymology</topic><topic>Subcellular Fractions - metabolism</topic><topic>Trophozoites</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kelsall, Brian L.</creatorcontrib><creatorcontrib>Ravdin, Jonathan I.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><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>The Journal of infectious diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kelsall, Brian L.</au><au>Ravdin, Jonathan I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Degradation of Human IgA by Entamoeba histolytica</atitle><jtitle>The Journal of infectious diseases</jtitle><addtitle>J Infect Dis</addtitle><date>1993-11-01</date><risdate>1993</risdate><volume>168</volume><issue>5</issue><spage>1319</spage><epage>1322</epage><pages>1319-1322</pages><issn>0022-1899</issn><eissn>1537-6613</eissn><coden>JIDIAQ</coden><abstract>To determine whether the virulent enteric pathogen Entamoeba histolytica degrades human IgA molecules, serum and secretory IgA was exposed to viable axenic trophozoites (strain HM1:IMSS), a parasite sonicate, and medium conditioned by incubation with live trophozoites. IgA was completely degraded under all conditions, proteinase activity was maximal at a neutral pH, and there was a four- to eightfold enrichment of amebic IgA proteolytic activity in a soluble fraction of amebic sonicate. Degradation of serum IgA by amebic sonicate was completely inhibited by the cysteine proteinase inhibitors trans-epoxysuccinyl-l-Ieucylamino(4-guanidino)butane (E-64, 100 µ,M) and benzyloxycarbonyl-phenyl-alanyl-alanyl-fluoromethyl ketone (Z-Phe-AlaCH2F, 12.5 µM). Secretion of degradative activity, the optimal pH, and the inhibition by E-64 and Z-Phe-Ala-CH2F indicates that cysteine proteinase activity is predominately responsible for the degradation of human IgA by E. histolytica.</abstract><cop>Chicago, IL</cop><pub>The University of Chicago Press</pub><pmid>8228372</pmid><doi>10.1093/infdis/168.5.1319</doi><tpages>4</tpages></addata></record> |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing |
| subjects | Animals Biological and medical sciences Concise Communications Cysteine Endopeptidases - metabolism Cysteine Proteinase Inhibitors - pharmacology Dipeptides - pharmacology Entamoeba histolytica Entamoeba histolytica - enzymology Entamoeba histolytica - metabolism Enzymes Epithelial cells Fundamental and applied biological sciences. Psychology Humans Immunoglobulin A - metabolism Immunoglobulins Infectious diseases Ketones - pharmacology Leucine - analogs & derivatives Leucine - pharmacology Life cycle. Host-agent relationship. Pathogenesis Mucus Parasites Particulate matter Protease inhibitors Protozoa Secretion Subcellular Fractions - enzymology Subcellular Fractions - metabolism Trophozoites |
| title | Degradation of Human IgA by Entamoeba histolytica |
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