Use of proteolytic enzymes as an additional tool for trypanosomatid identification
The expression of proteolytic activities in the Trypanosomatidae family was explored as a potential marker to discriminate between the morphologically indistinguishable flagellates isolated from insects and plants. We have comparatively analysed the proteolytic profiles of 19 monoxenous trypanosomat...
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| Veröffentlicht in: | Parasitology 2005-01, Vol.130 (1), p.79-88 |
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| creator | SANTOS, A. L. S. ABREU, C. M. ALVIANO, C. S. SOARES, R. M. A. |
| description | The expression of proteolytic activities in the Trypanosomatidae family was explored as a potential marker to discriminate between the morphologically indistinguishable flagellates isolated from insects and plants. We have comparatively analysed the proteolytic profiles of 19 monoxenous trypanosomatids (Herpetomonas anglusteri, H. samuelpessoai, H. mariadeanei, H. roitmani, H. muscarum ingenoplastis, H. muscarum muscarum, H. megaseliae, H. dendoderi, Herpetomoas sp., Crithidia oncopelti, C. deanei, C. acanthocephali, C. harmosa, C. fasciculata, C. guilhermei, C. luciliae, Blastocrithidia culicis, Leptomonas samueli and Lept. seymouri) and 4 heteroxenous flagellates (Phytomonas serpens, P. mcgheei, Trypanosoma cruzi and Leishmania amazonensis) by in situ detection of enzyme activities on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS–PAGE ) containing co-polymerized gelatine as substrate, in association with specific proteinase inhibitors. All 23 trypanosomatids expressed at least 1 acidic proteolytic enzyme. In addition, a characteristic and specific pattern of cell-associated metallo and/or cysteine proteinases was observed, except for the similar profiles detected in 2 Herpetomonas (H. anglusteri and H. samuelpessoai) and 3 Crithidia (C. fasciculata, C. guilhermei and C. luciliae) species. However, these flagellates released distinct secretory proteinase profiles into the extracellular medium. These findings strongly suggest that the association of cellular and secretory proteinase pattern could represent a useful marker to help trypanosomatid identification. |
| doi_str_mv | 10.1017/S0031182004006353 |
| format | Article |
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L. S. ; ABREU, C. M. ; ALVIANO, C. S. ; SOARES, R. M. A.</creator><creatorcontrib>SANTOS, A. L. S. ; ABREU, C. M. ; ALVIANO, C. S. ; SOARES, R. M. A.</creatorcontrib><description>The expression of proteolytic activities in the Trypanosomatidae family was explored as a potential marker to discriminate between the morphologically indistinguishable flagellates isolated from insects and plants. We have comparatively analysed the proteolytic profiles of 19 monoxenous trypanosomatids (Herpetomonas anglusteri, H. samuelpessoai, H. mariadeanei, H. roitmani, H. muscarum ingenoplastis, H. muscarum muscarum, H. megaseliae, H. dendoderi, Herpetomoas sp., Crithidia oncopelti, C. deanei, C. acanthocephali, C. harmosa, C. fasciculata, C. guilhermei, C. luciliae, Blastocrithidia culicis, Leptomonas samueli and Lept. seymouri) and 4 heteroxenous flagellates (Phytomonas serpens, P. mcgheei, Trypanosoma cruzi and Leishmania amazonensis) by in situ detection of enzyme activities on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS–PAGE ) containing co-polymerized gelatine as substrate, in association with specific proteinase inhibitors. All 23 trypanosomatids expressed at least 1 acidic proteolytic enzyme. In addition, a characteristic and specific pattern of cell-associated metallo and/or cysteine proteinases was observed, except for the similar profiles detected in 2 Herpetomonas (H. anglusteri and H. samuelpessoai) and 3 Crithidia (C. fasciculata, C. guilhermei and C. luciliae) species. However, these flagellates released distinct secretory proteinase profiles into the extracellular medium. These findings strongly suggest that the association of cellular and secretory proteinase pattern could represent a useful marker to help trypanosomatid identification.</description><identifier>ISSN: 0031-1820</identifier><identifier>EISSN: 1469-8161</identifier><identifier>DOI: 10.1017/S0031182004006353</identifier><identifier>PMID: 15700759</identifier><identifier>CODEN: PARAAE</identifier><language>eng</language><publisher>Cambridge, UK: Cambridge University Press</publisher><subject>Animals ; Biochemistry ; Biological and medical sciences ; Biomarkers ; cell-associated proteinases ; Copolymerization ; cysteine proteinases ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Enzymatic activity ; Enzymes ; Flagellates ; Fundamental and applied biological sciences. Psychology ; Gel electrophoresis ; Gelatin ; gelatine-polyacrylamide gel electrophoresis ; General aspects ; General aspects and techniques. Study of several systematic groups. Models ; Identification ; Insects ; Invertebrates ; Metallography ; metalloproteinases ; Parasites ; Parasitic diseases ; Parasitology ; Peptide Hydrolases - classification ; Peptide Hydrolases - metabolism ; Polypeptides ; Proteinase ; Proteinase inhibitors ; Proteolysis ; Proteolytic enzymes ; secretory proteinases ; Sodium dodecyl sulfate ; Sodium lauryl sulfate ; Species Specificity ; Substrate inhibition ; Trypanosomatidae ; Trypanosomatidae family ; Trypanosomatina - classification ; Trypanosomatina - enzymology</subject><ispartof>Parasitology, 2005-01, Vol.130 (1), p.79-88</ispartof><rights>2004 Cambridge University Press</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-ca40898479130fb4cc39c9fe6ffca7f405b6e445281487f68d0b1aa73ca29be73</citedby><cites>FETCH-LOGICAL-c470t-ca40898479130fb4cc39c9fe6ffca7f405b6e445281487f68d0b1aa73ca29be73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.cambridge.org/core/product/identifier/S0031182004006353/type/journal_article$$EHTML$$P50$$Gcambridge$$H</linktohtml><link.rule.ids>164,314,776,780,4010,27900,27901,27902,55603</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16571621$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15700759$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SANTOS, A. L. S.</creatorcontrib><creatorcontrib>ABREU, C. M.</creatorcontrib><creatorcontrib>ALVIANO, C. S.</creatorcontrib><creatorcontrib>SOARES, R. M. A.</creatorcontrib><title>Use of proteolytic enzymes as an additional tool for trypanosomatid identification</title><title>Parasitology</title><addtitle>Parasitology</addtitle><description>The expression of proteolytic activities in the Trypanosomatidae family was explored as a potential marker to discriminate between the morphologically indistinguishable flagellates isolated from insects and plants. We have comparatively analysed the proteolytic profiles of 19 monoxenous trypanosomatids (Herpetomonas anglusteri, H. samuelpessoai, H. mariadeanei, H. roitmani, H. muscarum ingenoplastis, H. muscarum muscarum, H. megaseliae, H. dendoderi, Herpetomoas sp., Crithidia oncopelti, C. deanei, C. acanthocephali, C. harmosa, C. fasciculata, C. guilhermei, C. luciliae, Blastocrithidia culicis, Leptomonas samueli and Lept. seymouri) and 4 heteroxenous flagellates (Phytomonas serpens, P. mcgheei, Trypanosoma cruzi and Leishmania amazonensis) by in situ detection of enzyme activities on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS–PAGE ) containing co-polymerized gelatine as substrate, in association with specific proteinase inhibitors. All 23 trypanosomatids expressed at least 1 acidic proteolytic enzyme. In addition, a characteristic and specific pattern of cell-associated metallo and/or cysteine proteinases was observed, except for the similar profiles detected in 2 Herpetomonas (H. anglusteri and H. samuelpessoai) and 3 Crithidia (C. fasciculata, C. guilhermei and C. luciliae) species. However, these flagellates released distinct secretory proteinase profiles into the extracellular medium. These findings strongly suggest that the association of cellular and secretory proteinase pattern could represent a useful marker to help trypanosomatid identification.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomarkers</subject><subject>cell-associated proteinases</subject><subject>Copolymerization</subject><subject>cysteine proteinases</subject><subject>Electrophoresis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymatic activity</subject><subject>Enzymes</subject><subject>Flagellates</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gel electrophoresis</subject><subject>Gelatin</subject><subject>gelatine-polyacrylamide gel electrophoresis</subject><subject>General aspects</subject><subject>General aspects and techniques. Study of several systematic groups. Models</subject><subject>Identification</subject><subject>Insects</subject><subject>Invertebrates</subject><subject>Metallography</subject><subject>metalloproteinases</subject><subject>Parasites</subject><subject>Parasitic diseases</subject><subject>Parasitology</subject><subject>Peptide Hydrolases - classification</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Polypeptides</subject><subject>Proteinase</subject><subject>Proteinase inhibitors</subject><subject>Proteolysis</subject><subject>Proteolytic enzymes</subject><subject>secretory proteinases</subject><subject>Sodium dodecyl sulfate</subject><subject>Sodium lauryl sulfate</subject><subject>Species Specificity</subject><subject>Substrate inhibition</subject><subject>Trypanosomatidae</subject><subject>Trypanosomatidae family</subject><subject>Trypanosomatina - classification</subject><subject>Trypanosomatina - enzymology</subject><issn>0031-1820</issn><issn>1469-8161</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkVFrFDEUhYModlv9Ab7IgNi3sbmTTDLzKEWrsFJWLYIv4U4mkdSZyTbJguuvb4YdXFCkEJKH891z78kl5AXQN0BBXnyhlAE0FaWcUsFq9oisgIu2bEDAY7Ka5XLWT8hpjLd0hkT1lJxALSmVdbsin2-iKbwttsEn44d9crow0-_9aGKB-UwF9r1Lzk84FMn7obA-FCnstzj56EdMri9cb6bkrNM4g8_IE4tDNM-X94zcvH_39fJDub6--nj5dl1qLmkqNXLatA2XLTBqO641a3VrjbBWo7Sc1p0wnNdVA7yRVjQ97QBRMo1V2xnJzsj5wTfPfrczManRRW2GASfjd1EJyUFCIx4EQYqaNmJ2fPUXeOt3ISePqsrfxfMlIFNwoHTwMQZj1Ta4EcNeAVXzXtQ_e8k1LxfnXTea_lixLCIDrxcAo8bBBpy0i0dO1BJENTcvD5yLyfz6o2P4mfMyWStxtVHfNuvN90-tUDPPlmFx7ILrf5hjpv-Pew-_vrLA</recordid><startdate>200501</startdate><enddate>200501</enddate><creator>SANTOS, A. 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L. S.</au><au>ABREU, C. M.</au><au>ALVIANO, C. S.</au><au>SOARES, R. M. A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Use of proteolytic enzymes as an additional tool for trypanosomatid identification</atitle><jtitle>Parasitology</jtitle><addtitle>Parasitology</addtitle><date>2005-01</date><risdate>2005</risdate><volume>130</volume><issue>1</issue><spage>79</spage><epage>88</epage><pages>79-88</pages><issn>0031-1820</issn><eissn>1469-8161</eissn><coden>PARAAE</coden><abstract>The expression of proteolytic activities in the Trypanosomatidae family was explored as a potential marker to discriminate between the morphologically indistinguishable flagellates isolated from insects and plants. We have comparatively analysed the proteolytic profiles of 19 monoxenous trypanosomatids (Herpetomonas anglusteri, H. samuelpessoai, H. mariadeanei, H. roitmani, H. muscarum ingenoplastis, H. muscarum muscarum, H. megaseliae, H. dendoderi, Herpetomoas sp., Crithidia oncopelti, C. deanei, C. acanthocephali, C. harmosa, C. fasciculata, C. guilhermei, C. luciliae, Blastocrithidia culicis, Leptomonas samueli and Lept. seymouri) and 4 heteroxenous flagellates (Phytomonas serpens, P. mcgheei, Trypanosoma cruzi and Leishmania amazonensis) by in situ detection of enzyme activities on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS–PAGE ) containing co-polymerized gelatine as substrate, in association with specific proteinase inhibitors. All 23 trypanosomatids expressed at least 1 acidic proteolytic enzyme. In addition, a characteristic and specific pattern of cell-associated metallo and/or cysteine proteinases was observed, except for the similar profiles detected in 2 Herpetomonas (H. anglusteri and H. samuelpessoai) and 3 Crithidia (C. fasciculata, C. guilhermei and C. luciliae) species. However, these flagellates released distinct secretory proteinase profiles into the extracellular medium. These findings strongly suggest that the association of cellular and secretory proteinase pattern could represent a useful marker to help trypanosomatid identification.</abstract><cop>Cambridge, UK</cop><pub>Cambridge University Press</pub><pmid>15700759</pmid><doi>10.1017/S0031182004006353</doi><tpages>10</tpages></addata></record> |
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| subjects | Animals Biochemistry Biological and medical sciences Biomarkers cell-associated proteinases Copolymerization cysteine proteinases Electrophoresis Electrophoresis, Polyacrylamide Gel Enzymatic activity Enzymes Flagellates Fundamental and applied biological sciences. Psychology Gel electrophoresis Gelatin gelatine-polyacrylamide gel electrophoresis General aspects General aspects and techniques. Study of several systematic groups. Models Identification Insects Invertebrates Metallography metalloproteinases Parasites Parasitic diseases Parasitology Peptide Hydrolases - classification Peptide Hydrolases - metabolism Polypeptides Proteinase Proteinase inhibitors Proteolysis Proteolytic enzymes secretory proteinases Sodium dodecyl sulfate Sodium lauryl sulfate Species Specificity Substrate inhibition Trypanosomatidae Trypanosomatidae family Trypanosomatina - classification Trypanosomatina - enzymology |
| title | Use of proteolytic enzymes as an additional tool for trypanosomatid identification |
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