Rapid identification of clinical Trichoderma longibrachiatum isolates by cellulose-acetate electrophoresis-mediated isoenzyme analysis
Cellulose-acetate electrophoresis was used to investigate isoenzyme polymorphism among ten clinical and 11 non-clinical isolates of Trichoderma. Initial testing of 13 enzyme systems for activity and resolution of bands showed that seven were appropriate for identifying the different species. Each of...
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Veröffentlicht in: | Clinical microbiology and infection 2006-04, Vol.12 (4), p.369-375 |
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description | Cellulose-acetate electrophoresis was used to investigate isoenzyme polymorphism among ten clinical and 11 non-clinical isolates of Trichoderma. Initial testing of 13 enzyme systems for activity and resolution of bands showed that seven were appropriate for identifying the different species. Each of the enzyme systems investigated (glucose-6-phosphate dehydrogenase, glucose-6-phosphate isomerase, 6-phosphogluconate dehydrogenase, peptidases A, B and D, and phosphoglucomutase) was diagnostic for at least one species. On the basis of the results of isoenzyme analysis, several isolates identified originally as Trichoderma pseudokoningii, T. koningii or T. citrinoviride were re-identified as T. longibrachiatum, in agreement with sequence analysis data for the internal transcribed spacer region of the isolates. The availability of a quick, inexpensive and reliable diagnostic tool for the identification of T. longibrachiatum isolates is important, as most clinical Trichoderma isolates belong to T. longibrachiatum. Furthermore, as many different enzyme systems are available, the method may also be suitable for the identification of other clinically relevant fungal species. |
doi_str_mv | 10.1111/j.1469-0691.2005.01356.x |
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Initial testing of 13 enzyme systems for activity and resolution of bands showed that seven were appropriate for identifying the different species. Each of the enzyme systems investigated (glucose-6-phosphate dehydrogenase, glucose-6-phosphate isomerase, 6-phosphogluconate dehydrogenase, peptidases A, B and D, and phosphoglucomutase) was diagnostic for at least one species. On the basis of the results of isoenzyme analysis, several isolates identified originally as Trichoderma pseudokoningii, T. koningii or T. citrinoviride were re-identified as T. longibrachiatum, in agreement with sequence analysis data for the internal transcribed spacer region of the isolates. The availability of a quick, inexpensive and reliable diagnostic tool for the identification of T. longibrachiatum isolates is important, as most clinical Trichoderma isolates belong to T. longibrachiatum. 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Initial testing of 13 enzyme systems for activity and resolution of bands showed that seven were appropriate for identifying the different species. Each of the enzyme systems investigated (glucose-6-phosphate dehydrogenase, glucose-6-phosphate isomerase, 6-phosphogluconate dehydrogenase, peptidases A, B and D, and phosphoglucomutase) was diagnostic for at least one species. On the basis of the results of isoenzyme analysis, several isolates identified originally as Trichoderma pseudokoningii, T. koningii or T. citrinoviride were re-identified as T. longibrachiatum, in agreement with sequence analysis data for the internal transcribed spacer region of the isolates. The availability of a quick, inexpensive and reliable diagnostic tool for the identification of T. longibrachiatum isolates is important, as most clinical Trichoderma isolates belong to T. longibrachiatum. Furthermore, as many different enzyme systems are available, the method may also be suitable for the identification of other clinically relevant fungal species.</description><subject>Biological and medical sciences</subject><subject>Cellulose-acetate electrophoresis</subject><subject>diagnosis</subject><subject>Electrophoresis, Cellulose Acetate - methods</subject><subject>Fungal Proteins - analysis</subject><subject>Fungal Proteins - classification</subject><subject>Humans</subject><subject>identification of fungi</subject><subject>Infectious diseases</subject><subject>isoenzyme analysis</subject><subject>Isoenzymes - analysis</subject><subject>Isoenzymes - classification</subject><subject>Medical sciences</subject><subject>Mycoses - microbiology</subject><subject>Phylogeny</subject><subject>Trichoderma - cytology</subject><subject>Trichoderma - enzymology</subject><subject>Trichoderma - isolation & purification</subject><subject>Trichoderma koningii</subject><subject>Trichoderma longibrachiatum</subject><subject>Trichoderma spp</subject><issn>1198-743X</issn><issn>1469-0691</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc9u1DAQxiNERUvhFZAvcEuwY8dODhxgxT9pK6SqlbhZE2fCeuXEi51AwwPw3Djsih6LLzNjf589nl-WEUYLltbrfcGEbHIqG1aUlFYFZbySxd2j7OLfweOUs6bOleBfz7OnMe4ppSXn4kl2zmRVCsHERfb7Gg62I7bDcbK9NTBZPxLfE-PsmEpHboI1O99hGIA4P36zbQCzszDNA7HRO5gwknYhBp2bnY-Yg8Ep7RJ0aKbgDzsfMNqYD9glG3arDcdfy4AERnBLOnuWnfXgIj4_xcvs9sP7m82nfPvl4-fN221uKq5k3hjagmSqYaIRwBFE33doetFxFJwxAA5tyaUwNai2SxEVpEIh9Iic88vs1fHeQ_DfZ4yTHmxcO4cR_Ry1VKpsmKwfFDLFKlnXq7A-Ck3wMQbs9SHYAcKiGdUrLL3XKxO9MtErLP0Xlr5L1henN-Y2zebeeKKTBC9PAogJRR9gNDbe61QlyoY2SffmqPtpHS7_3YDebK_WLPnfHf2YRv_DYtDRWBxN4hUSQt15-_Bv_gBFmMoV</recordid><startdate>200604</startdate><enddate>200604</enddate><creator>Szekeres, A.</creator><creator>Láday, M.</creator><creator>Kredics, L.</creator><creator>Varga, J.</creator><creator>Antal, Z.</creator><creator>Hatvani, L.</creator><creator>Manczinger, L.</creator><creator>Vágvölgyi, C.</creator><creator>Nagy, E.</creator><general>Elsevier Ltd</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>6I.</scope><scope>AAFTH</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>200604</creationdate><title>Rapid identification of clinical Trichoderma longibrachiatum isolates by cellulose-acetate electrophoresis-mediated isoenzyme analysis</title><author>Szekeres, A. ; 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Initial testing of 13 enzyme systems for activity and resolution of bands showed that seven were appropriate for identifying the different species. Each of the enzyme systems investigated (glucose-6-phosphate dehydrogenase, glucose-6-phosphate isomerase, 6-phosphogluconate dehydrogenase, peptidases A, B and D, and phosphoglucomutase) was diagnostic for at least one species. On the basis of the results of isoenzyme analysis, several isolates identified originally as Trichoderma pseudokoningii, T. koningii or T. citrinoviride were re-identified as T. longibrachiatum, in agreement with sequence analysis data for the internal transcribed spacer region of the isolates. The availability of a quick, inexpensive and reliable diagnostic tool for the identification of T. longibrachiatum isolates is important, as most clinical Trichoderma isolates belong to T. longibrachiatum. 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subjects | Biological and medical sciences Cellulose-acetate electrophoresis diagnosis Electrophoresis, Cellulose Acetate - methods Fungal Proteins - analysis Fungal Proteins - classification Humans identification of fungi Infectious diseases isoenzyme analysis Isoenzymes - analysis Isoenzymes - classification Medical sciences Mycoses - microbiology Phylogeny Trichoderma - cytology Trichoderma - enzymology Trichoderma - isolation & purification Trichoderma koningii Trichoderma longibrachiatum Trichoderma spp |
title | Rapid identification of clinical Trichoderma longibrachiatum isolates by cellulose-acetate electrophoresis-mediated isoenzyme analysis |
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