A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins
A neutral metalloprotease with marked specificity for an O-sialoglycoprotein has been isolated from culture supernatants of Pasteurella haemolytica A1. The 35-kDa enzyme cleaves human erythrocyte glycophorin A, which is O glycosylated, but does not cleave N-glycosylated proteins or nonglycosylated p...
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| Veröffentlicht in: | Infection and Immunity 1992-01, Vol.60 (1), p.56-62 |
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| creator | Abdullah, K.M. (Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario, Canada) Udoh, E.A Shewen, P.E Mellors, A |
| description | A neutral metalloprotease with marked specificity for an O-sialoglycoprotein has been isolated from culture supernatants of Pasteurella haemolytica A1. The 35-kDa enzyme cleaves human erythrocyte glycophorin A, which is O glycosylated, but does not cleave N-glycosylated proteins or nonglycosylated proteins. Glycophorin A was cleaved when it was present in situ in erythrocyte ghost plasma membranes or when it was free in solution. The glycoprotease did not hydrolyze glycophorin A from which sialate residues had been removed by neuraminidase treatment. An immobilized preparation of the enzyme cleaved glycophorin A at several positions, with a major site of cleavage at Arg-31-Asp-32. The glycoprotease is inhibited by EDTA, citrate, and ascorbate, but inhibition appears to be due to the masking of metal ion activators rather than to their removal. The enzyme is not inhibited by phosphoramidon, an inhibitor of other bacterial neutral metalloproteases |
| doi_str_mv | 10.1128/iai.60.1.56-62.1992 |
| format | Article |
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(Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario, Canada) ; Udoh, E.A ; Shewen, P.E ; Mellors, A</creator><creatorcontrib>Abdullah, K.M. (Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario, Canada) ; Udoh, E.A ; Shewen, P.E ; Mellors, A</creatorcontrib><description>A neutral metalloprotease with marked specificity for an O-sialoglycoprotein has been isolated from culture supernatants of Pasteurella haemolytica A1. The 35-kDa enzyme cleaves human erythrocyte glycophorin A, which is O glycosylated, but does not cleave N-glycosylated proteins or nonglycosylated proteins. Glycophorin A was cleaved when it was present in situ in erythrocyte ghost plasma membranes or when it was free in solution. The glycoprotease did not hydrolyze glycophorin A from which sialate residues had been removed by neuraminidase treatment. An immobilized preparation of the enzyme cleaved glycophorin A at several positions, with a major site of cleavage at Arg-31-Asp-32. The glycoprotease is inhibited by EDTA, citrate, and ascorbate, but inhibition appears to be due to the masking of metal ion activators rather than to their removal. The enzyme is not inhibited by phosphoramidon, an inhibitor of other bacterial neutral metalloproteases</description><identifier>ISSN: 0019-9567</identifier><identifier>EISSN: 1098-5522</identifier><identifier>DOI: 10.1128/iai.60.1.56-62.1992</identifier><identifier>PMID: 1729196</identifier><identifier>CODEN: INFIBR</identifier><language>eng</language><publisher>WASHINGTON: American Society for Microbiology</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Ascorbic Acid - pharmacology ; Bacteriology ; Biological and medical sciences ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Citrates - pharmacology ; Citric Acid ; Edetic Acid - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; GLICOPROTEINAS ; Glycopeptides - pharmacology ; Glycophorin - metabolism ; GLYCOPROTEINE ; Humans ; Hydrolysis - drug effects ; Immunology ; In Vitro Techniques ; Infectious Diseases ; INHIBIDORES DE ENZIMAS ; INHIBITEUR D'ENZYME ; Life Sciences & Biomedicine ; Mannheimia haemolytica - enzymology ; Metabolism. Enzymes ; Metalloendopeptidases - isolation & purification ; Metalloendopeptidases - physiology ; Microbiology ; Neuraminidase - pharmacology ; PASTEURELLA ; PROPIEDADES FISICO-QUIMICAS ; PROPRIETE PHYSICOCHIMIQUE ; PROTEASAS ; PROTEASE ; PURIFICACION ; PURIFICATION ; Science & Technology ; Sialoglycoproteins - metabolism ; Substrate Specificity</subject><ispartof>Infection and Immunity, 1992-01, Vol.60 (1), p.56-62</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>119</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wosA1992GW97400009</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c537t-bce98e66194d33154e07acabdcf05158419c0ff12703d1c904e8817f4764129d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC257502/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC257502/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,3189,3190,4025,27197,27928,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5109187$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1729196$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abdullah, K.M. (Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario, Canada)</creatorcontrib><creatorcontrib>Udoh, E.A</creatorcontrib><creatorcontrib>Shewen, P.E</creatorcontrib><creatorcontrib>Mellors, A</creatorcontrib><title>A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins</title><title>Infection and Immunity</title><addtitle>INFECT IMMUN</addtitle><addtitle>Infect Immun</addtitle><description>A neutral metalloprotease with marked specificity for an O-sialoglycoprotein has been isolated from culture supernatants of Pasteurella haemolytica A1. The 35-kDa enzyme cleaves human erythrocyte glycophorin A, which is O glycosylated, but does not cleave N-glycosylated proteins or nonglycosylated proteins. Glycophorin A was cleaved when it was present in situ in erythrocyte ghost plasma membranes or when it was free in solution. The glycoprotease did not hydrolyze glycophorin A from which sialate residues had been removed by neuraminidase treatment. An immobilized preparation of the enzyme cleaved glycophorin A at several positions, with a major site of cleavage at Arg-31-Asp-32. The glycoprotease is inhibited by EDTA, citrate, and ascorbate, but inhibition appears to be due to the masking of metal ion activators rather than to their removal. The enzyme is not inhibited by phosphoramidon, an inhibitor of other bacterial neutral metalloproteases</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Ascorbic Acid - pharmacology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Gel</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Ion Exchange</subject><subject>Citrates - pharmacology</subject><subject>Citric Acid</subject><subject>Edetic Acid - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GLICOPROTEINAS</subject><subject>Glycopeptides - pharmacology</subject><subject>Glycophorin - metabolism</subject><subject>GLYCOPROTEINE</subject><subject>Humans</subject><subject>Hydrolysis - drug effects</subject><subject>Immunology</subject><subject>In Vitro Techniques</subject><subject>Infectious Diseases</subject><subject>INHIBIDORES DE ENZIMAS</subject><subject>INHIBITEUR D'ENZYME</subject><subject>Life Sciences & Biomedicine</subject><subject>Mannheimia haemolytica - enzymology</subject><subject>Metabolism. Enzymes</subject><subject>Metalloendopeptidases - isolation & purification</subject><subject>Metalloendopeptidases - physiology</subject><subject>Microbiology</subject><subject>Neuraminidase - pharmacology</subject><subject>PASTEURELLA</subject><subject>PROPIEDADES FISICO-QUIMICAS</subject><subject>PROPRIETE PHYSICOCHIMIQUE</subject><subject>PROTEASAS</subject><subject>PROTEASE</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Science & Technology</subject><subject>Sialoglycoproteins - metabolism</subject><subject>Substrate Specificity</subject><issn>0019-9567</issn><issn>1098-5522</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EZCTM</sourceid><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhiMEKkvhD4AQOaBeUBbb8eeBw2pFC1KlIkHF0fI6412jJN7aSav99zjKaltu-OIZzfPaM_MWxTuMlhgT-dkbv-Q5XjJecbLESpFnxQIjJSvGCHleLBDCqlKMi5fFq5T-5JRSKs-KMyyIwoovCr0qexiHaNpy2x5s2McwgElQBlf-MGmAMULbmnJnoAvtYfDWlCtcpj1Y73LStofStmDuIZU3VfKmDY_v-D69Ll440yZ4c7zPi9vLr7_W36rrm6vv69V1ZVkthmpjQUngHCva1DVmFJAw1mwa6xDDTFKsLHIOE4HqBluFKEiJhaOCU0xUU58XX-Z39-Omg8ZCP82k99F3Jh50MF7_W-n9Tm_DvSZMMESy_uKoj-FuhDTozic7jd5DGJMWRGCVl5bBegZtDClFcKc_MNKTLTrbonmONeOaEz3ZklXvn7b3qJl9yPWPx7pJeakumt76dMJYNhVLkTE5Yw-wCS5ZD72FE7Wavrr6rQRF-ai1H8zgQ78OYz9k6af_l2b6w0zv_Hb34CNok7qnk2Xi7Uw4E7TZxtzt7U9VE0Elqf8CErzMxA</recordid><startdate>199201</startdate><enddate>199201</enddate><creator>Abdullah, K.M. (Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario, Canada)</creator><creator>Udoh, E.A</creator><creator>Shewen, P.E</creator><creator>Mellors, A</creator><general>American Society for Microbiology</general><general>Amer Soc Microbiology</general><scope>FBQ</scope><scope>BLEPL</scope><scope>DTL</scope><scope>EZCTM</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>199201</creationdate><title>A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins</title><author>Abdullah, K.M. (Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario, Canada) ; Udoh, E.A ; Shewen, P.E ; Mellors, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c537t-bce98e66194d33154e07acabdcf05158419c0ff12703d1c904e8817f4764129d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Ascorbic Acid - pharmacology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Gel</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Ion Exchange</topic><topic>Citrates - pharmacology</topic><topic>Citric Acid</topic><topic>Edetic Acid - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GLICOPROTEINAS</topic><topic>Glycopeptides - pharmacology</topic><topic>Glycophorin - metabolism</topic><topic>GLYCOPROTEINE</topic><topic>Humans</topic><topic>Hydrolysis - drug effects</topic><topic>Immunology</topic><topic>In Vitro Techniques</topic><topic>Infectious Diseases</topic><topic>INHIBIDORES DE ENZIMAS</topic><topic>INHIBITEUR D'ENZYME</topic><topic>Life Sciences & Biomedicine</topic><topic>Mannheimia haemolytica - enzymology</topic><topic>Metabolism. Enzymes</topic><topic>Metalloendopeptidases - isolation & purification</topic><topic>Metalloendopeptidases - physiology</topic><topic>Microbiology</topic><topic>Neuraminidase - pharmacology</topic><topic>PASTEURELLA</topic><topic>PROPIEDADES FISICO-QUIMICAS</topic><topic>PROPRIETE PHYSICOCHIMIQUE</topic><topic>PROTEASAS</topic><topic>PROTEASE</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Science & Technology</topic><topic>Sialoglycoproteins - metabolism</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Abdullah, K.M. (Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario, Canada)</creatorcontrib><creatorcontrib>Udoh, E.A</creatorcontrib><creatorcontrib>Shewen, P.E</creatorcontrib><creatorcontrib>Mellors, A</creatorcontrib><collection>AGRIS</collection><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 1992</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Infection and Immunity</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abdullah, K.M. (Guelph-Waterloo Centre for Graduate Work in Chemistry, Ontario, Canada)</au><au>Udoh, E.A</au><au>Shewen, P.E</au><au>Mellors, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins</atitle><jtitle>Infection and Immunity</jtitle><stitle>INFECT IMMUN</stitle><addtitle>Infect Immun</addtitle><date>1992-01</date><risdate>1992</risdate><volume>60</volume><issue>1</issue><spage>56</spage><epage>62</epage><pages>56-62</pages><issn>0019-9567</issn><eissn>1098-5522</eissn><coden>INFIBR</coden><abstract>A neutral metalloprotease with marked specificity for an O-sialoglycoprotein has been isolated from culture supernatants of Pasteurella haemolytica A1. The 35-kDa enzyme cleaves human erythrocyte glycophorin A, which is O glycosylated, but does not cleave N-glycosylated proteins or nonglycosylated proteins. Glycophorin A was cleaved when it was present in situ in erythrocyte ghost plasma membranes or when it was free in solution. The glycoprotease did not hydrolyze glycophorin A from which sialate residues had been removed by neuraminidase treatment. An immobilized preparation of the enzyme cleaved glycophorin A at several positions, with a major site of cleavage at Arg-31-Asp-32. The glycoprotease is inhibited by EDTA, citrate, and ascorbate, but inhibition appears to be due to the masking of metal ion activators rather than to their removal. The enzyme is not inhibited by phosphoramidon, an inhibitor of other bacterial neutral metalloproteases</abstract><cop>WASHINGTON</cop><pub>American Society for Microbiology</pub><pmid>1729196</pmid><doi>10.1128/iai.60.1.56-62.1992</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | Web of Science - Science Citation Index Expanded - 1992<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; American Society for Microbiology; MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Ascorbic Acid - pharmacology Bacteriology Biological and medical sciences Chromatography, Gel Chromatography, High Pressure Liquid Chromatography, Ion Exchange Citrates - pharmacology Citric Acid Edetic Acid - pharmacology Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology GLICOPROTEINAS Glycopeptides - pharmacology Glycophorin - metabolism GLYCOPROTEINE Humans Hydrolysis - drug effects Immunology In Vitro Techniques Infectious Diseases INHIBIDORES DE ENZIMAS INHIBITEUR D'ENZYME Life Sciences & Biomedicine Mannheimia haemolytica - enzymology Metabolism. Enzymes Metalloendopeptidases - isolation & purification Metalloendopeptidases - physiology Microbiology Neuraminidase - pharmacology PASTEURELLA PROPIEDADES FISICO-QUIMICAS PROPRIETE PHYSICOCHIMIQUE PROTEASAS PROTEASE PURIFICACION PURIFICATION Science & Technology Sialoglycoproteins - metabolism Substrate Specificity |
| title | A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins |
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