The Human-Specific Action of Intermedilysin, a Homolog of Streptolysin O, Is Dictated by Domain 4 of the Protein
Intermedilysin is a pore‐forming cytolysin belonging to the streptolysin O gene family known as the ‘Cholesterol‐binding/dependent cytolysins’ and is unique within the family in that it is highly human‐specific. This specificity suggests interaction with a component of human cells other than cholest...
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| Veröffentlicht in: | Microbiology and immunology 2004-01, Vol.48 (9), p.677-692 |
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| container_title | Microbiology and immunology |
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| creator | Nagamune, Hideaki Ohkura, Kazuto Sukeno, Akiko Cowan, Graeme Mitchell, Timothy J. Ito, Wataru Ohnishi, Ooki Hattori, Kanako Yamato, Miki Hirota, Katsuhiko Miyake, Yoichiro Maeda, Takuya Kourai, Hiroki |
| description | Intermedilysin is a pore‐forming cytolysin belonging to the streptolysin O gene family known as the ‘Cholesterol‐binding/dependent cytolysins’ and is unique within the family in that it is highly human‐specific. This specificity suggests interaction with a component of human cells other than cholesterol, the proposed receptor for the other toxins of the gene family. Indeed, intermedilysin showed no significant degree of affinity to free or liposome‐embedded cholesterol. Characterization of intermedilysin undecapeptide mutants revealed that this lack of affinity to cholesterol was a result of the substitutions of intermedilysin in this region. Absorption assays with erythrocyte membranes from various animals, competitive inhibition with domain 4 of intermedilysin and liposome‐binding assays of streptolysin O and intermedilysin indicated that cell membrane binding is the human‐specific step of intermedilysin action, that the host cell membrane‐binding site is located within domain 4 in common with other members of the family and that the receptor for this toxin is not cholesterol. The species specificity of undecapeptide mutants of intermedilysin and streptolysin O and chimeric mutants between intermedilysin and streptolysin O, and intermedilysin and pneumolysin indicated that domain 4 of intermedilysin determines the human‐specific action step and the cell‐binding site of domain 4 lies within the 56 amino acids of the C‐terminal, excluding the undecapeptide region. |
| doi_str_mv | 10.1111/j.1348-0421.2004.tb03479.x |
| format | Article |
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This specificity suggests interaction with a component of human cells other than cholesterol, the proposed receptor for the other toxins of the gene family. Indeed, intermedilysin showed no significant degree of affinity to free or liposome‐embedded cholesterol. Characterization of intermedilysin undecapeptide mutants revealed that this lack of affinity to cholesterol was a result of the substitutions of intermedilysin in this region. Absorption assays with erythrocyte membranes from various animals, competitive inhibition with domain 4 of intermedilysin and liposome‐binding assays of streptolysin O and intermedilysin indicated that cell membrane binding is the human‐specific step of intermedilysin action, that the host cell membrane‐binding site is located within domain 4 in common with other members of the family and that the receptor for this toxin is not cholesterol. The species specificity of undecapeptide mutants of intermedilysin and streptolysin O and chimeric mutants between intermedilysin and streptolysin O, and intermedilysin and pneumolysin indicated that domain 4 of intermedilysin determines the human‐specific action step and the cell‐binding site of domain 4 lies within the 56 amino acids of the C‐terminal, excluding the undecapeptide region.</description><identifier>ISSN: 0385-5600</identifier><identifier>EISSN: 1348-0421</identifier><identifier>DOI: 10.1111/j.1348-0421.2004.tb03479.x</identifier><identifier>PMID: 15383705</identifier><language>eng</language><publisher>Australia: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriocins ; Binding Sites ; Cholesterol - metabolism ; Erythrocyte Membrane - metabolism ; hemolysin ; Hemolysis ; human-specific ; Humans ; intermedilysin ; Liposomes ; Microscopy, Electron, Transmission ; Models, Molecular ; Molecular Sequence Data ; Point Mutation ; pore-forming toxin ; Rabbits ; Species Specificity ; Streptococcus intermedius - genetics ; Streptococcus intermedius - metabolism ; Streptolysins - genetics</subject><ispartof>Microbiology and immunology, 2004-01, Vol.48 (9), p.677-692</ispartof><rights>owned by Center for Academic Publications Japan (Publisher)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5259-a1f011b3bee508c815fb452f6f1e42e63786eab23617c68b1f64f4b838599a573</citedby><cites>FETCH-LOGICAL-c5259-a1f011b3bee508c815fb452f6f1e42e63786eab23617c68b1f64f4b838599a573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1348-0421.2004.tb03479.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1348-0421.2004.tb03479.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15383705$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nagamune, Hideaki</creatorcontrib><creatorcontrib>Ohkura, Kazuto</creatorcontrib><creatorcontrib>Sukeno, Akiko</creatorcontrib><creatorcontrib>Cowan, Graeme</creatorcontrib><creatorcontrib>Mitchell, Timothy J.</creatorcontrib><creatorcontrib>Ito, Wataru</creatorcontrib><creatorcontrib>Ohnishi, Ooki</creatorcontrib><creatorcontrib>Hattori, Kanako</creatorcontrib><creatorcontrib>Yamato, Miki</creatorcontrib><creatorcontrib>Hirota, Katsuhiko</creatorcontrib><creatorcontrib>Miyake, Yoichiro</creatorcontrib><creatorcontrib>Maeda, Takuya</creatorcontrib><creatorcontrib>Kourai, Hiroki</creatorcontrib><title>The Human-Specific Action of Intermedilysin, a Homolog of Streptolysin O, Is Dictated by Domain 4 of the Protein</title><title>Microbiology and immunology</title><addtitle>Microbiology and Immunology</addtitle><description>Intermedilysin is a pore‐forming cytolysin belonging to the streptolysin O gene family known as the ‘Cholesterol‐binding/dependent cytolysins’ and is unique within the family in that it is highly human‐specific. 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The species specificity of undecapeptide mutants of intermedilysin and streptolysin O and chimeric mutants between intermedilysin and streptolysin O, and intermedilysin and pneumolysin indicated that domain 4 of intermedilysin determines the human‐specific action step and the cell‐binding site of domain 4 lies within the 56 amino acids of the C‐terminal, excluding the undecapeptide region.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriocins</subject><subject>Binding Sites</subject><subject>Cholesterol - metabolism</subject><subject>Erythrocyte Membrane - metabolism</subject><subject>hemolysin</subject><subject>Hemolysis</subject><subject>human-specific</subject><subject>Humans</subject><subject>intermedilysin</subject><subject>Liposomes</subject><subject>Microscopy, Electron, Transmission</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Point Mutation</subject><subject>pore-forming toxin</subject><subject>Rabbits</subject><subject>Species Specificity</subject><subject>Streptococcus intermedius - genetics</subject><subject>Streptococcus intermedius - metabolism</subject><subject>Streptolysins - genetics</subject><issn>0385-5600</issn><issn>1348-0421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkM1u1DAURi0EokPhFZDFglUT_J-EFVULnYEpLWpR2VmOew2eJnGIPerM2zfpjMoab2zp--658kHoHSU5Hc-HVU65KDMiGM0ZISJPNeGiqPLNMzR7ip6jGeGlzKQi5AC9inFFCCtYKV6iAyp5yQsiZ6i__gN4vm5Nl131YL3zFh_b5EOHg8OLLsHQwq1vttF3R9jgeWhDE35P4VUaoE_hMcIXR3gR8am3ySS4xfUWn4bWjIGYqmlccjmEBL57jV4400R4s78P0c8vn69P5tny4mxxcrzMrGSyygx1hNKa1wCSlLak0tVCMqccBcFA8aJUYGrGFS2sKmvqlHCiLscfV5WRBT9E73fcfgh_1xCTbn200DSmg7COWqmKMMrlWPy4K9ohxDiA0_3gWzNsNSV68q1XepKqJ6l68q33vvVmHH6737KuR0__RveCx8KnXeHeN7D9D7Q-X5w_PkdEtkP4mGDzhDDDnVYFL6S--X6m2dcf325-LZf6kj8Aameeog</recordid><startdate>20040101</startdate><enddate>20040101</enddate><creator>Nagamune, Hideaki</creator><creator>Ohkura, Kazuto</creator><creator>Sukeno, Akiko</creator><creator>Cowan, Graeme</creator><creator>Mitchell, Timothy J.</creator><creator>Ito, Wataru</creator><creator>Ohnishi, Ooki</creator><creator>Hattori, Kanako</creator><creator>Yamato, Miki</creator><creator>Hirota, Katsuhiko</creator><creator>Miyake, Yoichiro</creator><creator>Maeda, Takuya</creator><creator>Kourai, Hiroki</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</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></search><sort><creationdate>20040101</creationdate><title>The Human-Specific Action of Intermedilysin, a Homolog of Streptolysin O, Is Dictated by Domain 4 of the Protein</title><author>Nagamune, Hideaki ; Ohkura, Kazuto ; Sukeno, Akiko ; Cowan, Graeme ; Mitchell, Timothy J. ; Ito, Wataru ; Ohnishi, Ooki ; Hattori, Kanako ; Yamato, Miki ; Hirota, Katsuhiko ; Miyake, Yoichiro ; Maeda, Takuya ; Kourai, Hiroki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5259-a1f011b3bee508c815fb452f6f1e42e63786eab23617c68b1f64f4b838599a573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriocins</topic><topic>Binding Sites</topic><topic>Cholesterol - metabolism</topic><topic>Erythrocyte Membrane - metabolism</topic><topic>hemolysin</topic><topic>Hemolysis</topic><topic>human-specific</topic><topic>Humans</topic><topic>intermedilysin</topic><topic>Liposomes</topic><topic>Microscopy, Electron, Transmission</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Point Mutation</topic><topic>pore-forming toxin</topic><topic>Rabbits</topic><topic>Species Specificity</topic><topic>Streptococcus intermedius - genetics</topic><topic>Streptococcus intermedius - metabolism</topic><topic>Streptolysins - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagamune, Hideaki</creatorcontrib><creatorcontrib>Ohkura, Kazuto</creatorcontrib><creatorcontrib>Sukeno, Akiko</creatorcontrib><creatorcontrib>Cowan, Graeme</creatorcontrib><creatorcontrib>Mitchell, Timothy J.</creatorcontrib><creatorcontrib>Ito, Wataru</creatorcontrib><creatorcontrib>Ohnishi, Ooki</creatorcontrib><creatorcontrib>Hattori, Kanako</creatorcontrib><creatorcontrib>Yamato, Miki</creatorcontrib><creatorcontrib>Hirota, Katsuhiko</creatorcontrib><creatorcontrib>Miyake, Yoichiro</creatorcontrib><creatorcontrib>Maeda, Takuya</creatorcontrib><creatorcontrib>Kourai, Hiroki</creatorcontrib><collection>Istex</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><jtitle>Microbiology and immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nagamune, Hideaki</au><au>Ohkura, Kazuto</au><au>Sukeno, Akiko</au><au>Cowan, Graeme</au><au>Mitchell, Timothy J.</au><au>Ito, Wataru</au><au>Ohnishi, Ooki</au><au>Hattori, Kanako</au><au>Yamato, Miki</au><au>Hirota, Katsuhiko</au><au>Miyake, Yoichiro</au><au>Maeda, Takuya</au><au>Kourai, Hiroki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Human-Specific Action of Intermedilysin, a Homolog of Streptolysin O, Is Dictated by Domain 4 of the Protein</atitle><jtitle>Microbiology and immunology</jtitle><addtitle>Microbiology and Immunology</addtitle><date>2004-01-01</date><risdate>2004</risdate><volume>48</volume><issue>9</issue><spage>677</spage><epage>692</epage><pages>677-692</pages><issn>0385-5600</issn><eissn>1348-0421</eissn><abstract>Intermedilysin is a pore‐forming cytolysin belonging to the streptolysin O gene family known as the ‘Cholesterol‐binding/dependent cytolysins’ and is unique within the family in that it is highly human‐specific. This specificity suggests interaction with a component of human cells other than cholesterol, the proposed receptor for the other toxins of the gene family. Indeed, intermedilysin showed no significant degree of affinity to free or liposome‐embedded cholesterol. Characterization of intermedilysin undecapeptide mutants revealed that this lack of affinity to cholesterol was a result of the substitutions of intermedilysin in this region. Absorption assays with erythrocyte membranes from various animals, competitive inhibition with domain 4 of intermedilysin and liposome‐binding assays of streptolysin O and intermedilysin indicated that cell membrane binding is the human‐specific step of intermedilysin action, that the host cell membrane‐binding site is located within domain 4 in common with other members of the family and that the receptor for this toxin is not cholesterol. The species specificity of undecapeptide mutants of intermedilysin and streptolysin O and chimeric mutants between intermedilysin and streptolysin O, and intermedilysin and pneumolysin indicated that domain 4 of intermedilysin determines the human‐specific action step and the cell‐binding site of domain 4 lies within the 56 amino acids of the C‐terminal, excluding the undecapeptide region.</abstract><cop>Australia</cop><pub>Blackwell Publishing Ltd</pub><pmid>15383705</pmid><doi>10.1111/j.1348-0421.2004.tb03479.x</doi><tpages>16</tpages></addata></record> |
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| identifier | ISSN: 0385-5600 |
| ispartof | Microbiology and immunology, 2004-01, Vol.48 (9), p.677-692 |
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| language | eng |
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| source | MEDLINE; Wiley Journals; Wiley Free Content; Freely Accessible Japanese Titles; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriocins Binding Sites Cholesterol - metabolism Erythrocyte Membrane - metabolism hemolysin Hemolysis human-specific Humans intermedilysin Liposomes Microscopy, Electron, Transmission Models, Molecular Molecular Sequence Data Point Mutation pore-forming toxin Rabbits Species Specificity Streptococcus intermedius - genetics Streptococcus intermedius - metabolism Streptolysins - genetics |
| title | The Human-Specific Action of Intermedilysin, a Homolog of Streptolysin O, Is Dictated by Domain 4 of the Protein |
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