Zymography Analysis of Proteinase Activity Present in Leptospira
Leptospirosis is a major public health problem caused by spirochete Leptospira which is an extracellular pathogen. During infection and invasion, the bacteria cross the physical barriers and later it encounter with the host defence mechanism. These processes may involve proteolytic degradation of th...
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Veröffentlicht in: | Current microbiology 2011-03, Vol.62 (3), p.917-922 |
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description | Leptospirosis is a major public health problem caused by spirochete Leptospira which is an extracellular pathogen. During infection and invasion, the bacteria cross the physical barriers and later it encounter with the host defence mechanism. These processes may involve proteolytic degradation of the host tissue biomatrix. In an effort to understand the production and nature of Leptospiral proteinases, investigations were carried out using zymograpic methods. The results showed that the leptospires degrades different kind of protein substances such as gelatin, casein, and albumin. Gelatin zymography reveals that different serovars contain multiple gelatinases in the molecular weight range from 240 to 32 kDa. Studies using inhibitors suggested that the Leptospiral proteinases include metalloproteinases, serine or cysteine proteinases. The temperature sensitivity suggests that some of these proteinases are stable even at high temperatures. The presence of multiple gelatinases in Leptospira serovars suggests a critical role for these enzymes in Leptospiral invasion and pathogenesis. |
doi_str_mv | 10.1007/s00284-010-9810-3 |
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During infection and invasion, the bacteria cross the physical barriers and later it encounter with the host defence mechanism. These processes may involve proteolytic degradation of the host tissue biomatrix. In an effort to understand the production and nature of Leptospiral proteinases, investigations were carried out using zymograpic methods. The results showed that the leptospires degrades different kind of protein substances such as gelatin, casein, and albumin. Gelatin zymography reveals that different serovars contain multiple gelatinases in the molecular weight range from 240 to 32 kDa. Studies using inhibitors suggested that the Leptospiral proteinases include metalloproteinases, serine or cysteine proteinases. The temperature sensitivity suggests that some of these proteinases are stable even at high temperatures. The presence of multiple gelatinases in Leptospira serovars suggests a critical role for these enzymes in Leptospiral invasion and pathogenesis.</description><identifier>ISSN: 0343-8651</identifier><identifier>EISSN: 1432-0991</identifier><identifier>DOI: 10.1007/s00284-010-9810-3</identifier><identifier>PMID: 21057952</identifier><language>eng</language><publisher>New York: New York : Springer-Verlag</publisher><subject>Albumins - metabolism ; Bacteria ; Bacterial infections ; Barriers ; Biomedical and Life Sciences ; Biotechnology ; Caseins - metabolism ; Electrophoresis - methods ; Enzymes ; Gelatin - metabolism ; High temperature ; Leptospira ; Leptospira - enzymology ; Life Sciences ; Microbiology ; Molecular biology ; Molecular Weight ; Peptide Hydrolases - chemistry ; Peptide Hydrolases - metabolism ; Public health</subject><ispartof>Current microbiology, 2011-03, Vol.62 (3), p.917-922</ispartof><rights>Springer Science+Business Media, LLC 2010</rights><rights>Springer Science+Business Media, LLC 2011</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-4ff4c36f52ef13839bc03ef62b0b520385b3856a81f434c1f67590cfca3cc8013</citedby><cites>FETCH-LOGICAL-c426t-4ff4c36f52ef13839bc03ef62b0b520385b3856a81f434c1f67590cfca3cc8013</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00284-010-9810-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00284-010-9810-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21057952$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Madathiparambil, Madanan G</creatorcontrib><creatorcontrib>Cattavarayane, Sandhanakrishnan</creatorcontrib><creatorcontrib>Manickam, Gayathri D</creatorcontrib><creatorcontrib>Singh, Kavita</creatorcontrib><creatorcontrib>Perumana, Sudhakaran R</creatorcontrib><creatorcontrib>Sehgal, Subhash C</creatorcontrib><title>Zymography Analysis of Proteinase Activity Present in Leptospira</title><title>Current microbiology</title><addtitle>Curr Microbiol</addtitle><addtitle>Curr Microbiol</addtitle><description>Leptospirosis is a major public health problem caused by spirochete Leptospira which is an extracellular pathogen. During infection and invasion, the bacteria cross the physical barriers and later it encounter with the host defence mechanism. These processes may involve proteolytic degradation of the host tissue biomatrix. In an effort to understand the production and nature of Leptospiral proteinases, investigations were carried out using zymograpic methods. The results showed that the leptospires degrades different kind of protein substances such as gelatin, casein, and albumin. Gelatin zymography reveals that different serovars contain multiple gelatinases in the molecular weight range from 240 to 32 kDa. Studies using inhibitors suggested that the Leptospiral proteinases include metalloproteinases, serine or cysteine proteinases. The temperature sensitivity suggests that some of these proteinases are stable even at high temperatures. The presence of multiple gelatinases in Leptospira serovars suggests a critical role for these enzymes in Leptospiral invasion and pathogenesis.</description><subject>Albumins - metabolism</subject><subject>Bacteria</subject><subject>Bacterial infections</subject><subject>Barriers</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Caseins - metabolism</subject><subject>Electrophoresis - methods</subject><subject>Enzymes</subject><subject>Gelatin - metabolism</subject><subject>High temperature</subject><subject>Leptospira</subject><subject>Leptospira - enzymology</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Molecular biology</subject><subject>Molecular Weight</subject><subject>Peptide Hydrolases - chemistry</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Public health</subject><issn>0343-8651</issn><issn>1432-0991</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkUtr3DAUhUVoSSaPH9BNYrLpys29enikXYaQpoWBFpJsshGyIk0VZixH8gT876uJ0xa6KF3oCnS_cwTnEPIB4RMCzC8yAJW8BoRayTLYHpkhZ7QGpfAdmQHjrJaNwANymPMTAFIFuE8OKIKYK0Fn5PJh3MRVMv2PsVp0Zj3mkKvoq-8pDi50JrtqYYfwEoaxvLnsuqEKXbV0_RBzH5I5Ju-9WWd38nYfkfvP13dXX-rlt5uvV4tlbTlthpp7zy1rvKDOI5NMtRaY8w1toRUUmBRtOY2R6DnjFn0zFwqst4ZZKwHZEfk4-fYpPm9dHvQmZOvWa9O5uM1aNsUEFf0PUjClBENayPO_yKe4TSWFV6iRVLEdhBNkU8w5Oa_7FDYmjRpB72rQUw261KB3NWhWNKdvxtt24x5_K37lXgA6AbmsupVLf37-l-vZJPImarNKIev7W1qyAVSci9L8TwZQmdI</recordid><startdate>20110301</startdate><enddate>20110301</enddate><creator>Madathiparambil, Madanan G</creator><creator>Cattavarayane, Sandhanakrishnan</creator><creator>Manickam, Gayathri D</creator><creator>Singh, Kavita</creator><creator>Perumana, Sudhakaran R</creator><creator>Sehgal, Subhash C</creator><general>New York : Springer-Verlag</general><general>Springer-Verlag</general><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope></search><sort><creationdate>20110301</creationdate><title>Zymography Analysis of Proteinase Activity Present in Leptospira</title><author>Madathiparambil, Madanan G ; Cattavarayane, Sandhanakrishnan ; Manickam, Gayathri D ; Singh, Kavita ; Perumana, Sudhakaran R ; Sehgal, Subhash C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-4ff4c36f52ef13839bc03ef62b0b520385b3856a81f434c1f67590cfca3cc8013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Albumins - 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During infection and invasion, the bacteria cross the physical barriers and later it encounter with the host defence mechanism. These processes may involve proteolytic degradation of the host tissue biomatrix. In an effort to understand the production and nature of Leptospiral proteinases, investigations were carried out using zymograpic methods. The results showed that the leptospires degrades different kind of protein substances such as gelatin, casein, and albumin. Gelatin zymography reveals that different serovars contain multiple gelatinases in the molecular weight range from 240 to 32 kDa. Studies using inhibitors suggested that the Leptospiral proteinases include metalloproteinases, serine or cysteine proteinases. The temperature sensitivity suggests that some of these proteinases are stable even at high temperatures. The presence of multiple gelatinases in Leptospira serovars suggests a critical role for these enzymes in Leptospiral invasion and pathogenesis.</abstract><cop>New York</cop><pub>New York : Springer-Verlag</pub><pmid>21057952</pmid><doi>10.1007/s00284-010-9810-3</doi><tpages>6</tpages></addata></record> |
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subjects | Albumins - metabolism Bacteria Bacterial infections Barriers Biomedical and Life Sciences Biotechnology Caseins - metabolism Electrophoresis - methods Enzymes Gelatin - metabolism High temperature Leptospira Leptospira - enzymology Life Sciences Microbiology Molecular biology Molecular Weight Peptide Hydrolases - chemistry Peptide Hydrolases - metabolism Public health |
title | Zymography Analysis of Proteinase Activity Present in Leptospira |
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