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Novel Phenol-soluble Modulin Derivatives in Community-associated Methicillin-resistant Staphylococcus aureus Identified through Imaging Mass Spectrometry
Staphylococcus aureus causes a wide range of human disease ranging from localized skin and soft tissue infections to potentially lethal systemic infections. S. aureus has the biosynthetic ability to generate numerous virulence factors that assist in circumventing the innate immune system during dise...
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| Published in: | The Journal of biological chemistry 2012-04, Vol.287 (17), p.13889-13898 |
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| creator | Gonzalez, David J. Okumura, Cheryl Y. Hollands, Andrew Kersten, Roland Akong-Moore, Kathryn Pence, Morgan A. Malone, Cheryl L. Derieux, Jaclyn Moore, Bradley S. Horswill, Alexander R. Dixon, Jack E. Dorrestein, Pieter C. Nizet, Victor |
| description | Staphylococcus aureus causes a wide range of human disease ranging from localized skin and soft tissue infections to potentially lethal systemic infections. S. aureus has the biosynthetic ability to generate numerous virulence factors that assist in circumventing the innate immune system during disease pathogenesis. Recent studies have uncovered a set of extracellular peptides produced by community-associated methicillin-resistant S. aureus (CA-MRSA) with homology to the phenol-soluble modulins (PSMs) from Staphylococcus epidermidis. CA-MRSA PSMs contribute to skin infection and recruit and lyse neutrophils, and truncated versions of these peptides possess antimicrobial activity. In this study, novel CA-MRSA PSM derivatives were discovered by the use of microbial imaging mass spectrometry. The novel PSM derivatives are compared with their parent full-length peptides for changes in hemolytic, cytolytic, and neutrophil-stimulating activity. A potential contribution of the major S. aureus secreted protease aureolysin in processing PSMs is demonstrated. Finally, we show that PSM processing occurs in multiple CA-MRSA strains by structural confirmation of additional novel derivatives. This work demonstrates that IMS can serve as a useful tool to go beyond genome predictions and expand our understanding of the important family of small peptide virulence factors.
Background: Phenol-soluble modulins (PSMs) are small peptides of Staphylococcus aureus with immunosuppressive and antimicrobial properties.
Results: Imaging mass spectrometry (IMS) identified PSM derivatives with properties different from those of the parent forms.
Conclusion:S. aureus generates truncated PSMs with altered antimicrobial and immunostimulatory properties and aureolysin may contribute to processing of some PSMs.
Significance: Observations using the technology of IMS expand our understanding of S. aureus PSMs. |
| doi_str_mv | 10.1074/jbc.M112.349860 |
| format | article |
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Background: Phenol-soluble modulins (PSMs) are small peptides of Staphylococcus aureus with immunosuppressive and antimicrobial properties.
Results: Imaging mass spectrometry (IMS) identified PSM derivatives with properties different from those of the parent forms.
Conclusion:S. aureus generates truncated PSMs with altered antimicrobial and immunostimulatory properties and aureolysin may contribute to processing of some PSMs.
Significance: Observations using the technology of IMS expand our understanding of S. aureus PSMs.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M112.349860</identifier><identifier>PMID: 22371493</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Anti-Infective Agents - pharmacology ; Bacteria ; Bacterial Infections ; Bacterial Infections - metabolism ; Bacterial Proteins - chemistry ; Bacterial Toxins ; Bacterial Toxins - chemistry ; Erythrocytes - cytology ; Hemolysis ; Humans ; Imaging Mass Spectrometry ; Immunosuppressive Agents - pharmacology ; Mass Spectrometry (MS) ; Mass Spectrometry - methods ; Metalloendopeptidases - chemistry ; Methicillin-Resistant Staphylococcus aureus - metabolism ; Mice ; Microbiology ; Molecular Sequence Data ; Neutrophils - cytology ; Neutrophils - metabolism ; Phenol - chemistry ; Phenol-soluble Modulins (PSMs) ; Sequence Homology, Amino Acid ; Sheep ; Skin - metabolism ; Skin - microbiology ; Staphylococcal Skin Infections - microbiology ; Staphylococcus aureus ; Virulence Factors ; Virulence Factors - chemistry</subject><ispartof>The Journal of biological chemistry, 2012-04, Vol.287 (17), p.13889-13898</ispartof><rights>2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2012 by The American Society for Biochemistry and Molecular Biology, Inc. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-9c38a75913ca8c01dfba50a148b5eba58bff7fef4ea588554331f5c42e8152e3</citedby><cites>FETCH-LOGICAL-c443t-9c38a75913ca8c01dfba50a148b5eba58bff7fef4ea588554331f5c42e8152e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3340166/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3340166/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,733,786,790,891,27957,27958,53827,53829</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22371493$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gonzalez, David J.</creatorcontrib><creatorcontrib>Okumura, Cheryl Y.</creatorcontrib><creatorcontrib>Hollands, Andrew</creatorcontrib><creatorcontrib>Kersten, Roland</creatorcontrib><creatorcontrib>Akong-Moore, Kathryn</creatorcontrib><creatorcontrib>Pence, Morgan A.</creatorcontrib><creatorcontrib>Malone, Cheryl L.</creatorcontrib><creatorcontrib>Derieux, Jaclyn</creatorcontrib><creatorcontrib>Moore, Bradley S.</creatorcontrib><creatorcontrib>Horswill, Alexander R.</creatorcontrib><creatorcontrib>Dixon, Jack E.</creatorcontrib><creatorcontrib>Dorrestein, Pieter C.</creatorcontrib><creatorcontrib>Nizet, Victor</creatorcontrib><title>Novel Phenol-soluble Modulin Derivatives in Community-associated Methicillin-resistant Staphylococcus aureus Identified through Imaging Mass Spectrometry</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Staphylococcus aureus causes a wide range of human disease ranging from localized skin and soft tissue infections to potentially lethal systemic infections. S. aureus has the biosynthetic ability to generate numerous virulence factors that assist in circumventing the innate immune system during disease pathogenesis. Recent studies have uncovered a set of extracellular peptides produced by community-associated methicillin-resistant S. aureus (CA-MRSA) with homology to the phenol-soluble modulins (PSMs) from Staphylococcus epidermidis. CA-MRSA PSMs contribute to skin infection and recruit and lyse neutrophils, and truncated versions of these peptides possess antimicrobial activity. In this study, novel CA-MRSA PSM derivatives were discovered by the use of microbial imaging mass spectrometry. The novel PSM derivatives are compared with their parent full-length peptides for changes in hemolytic, cytolytic, and neutrophil-stimulating activity. A potential contribution of the major S. aureus secreted protease aureolysin in processing PSMs is demonstrated. Finally, we show that PSM processing occurs in multiple CA-MRSA strains by structural confirmation of additional novel derivatives. This work demonstrates that IMS can serve as a useful tool to go beyond genome predictions and expand our understanding of the important family of small peptide virulence factors.
Background: Phenol-soluble modulins (PSMs) are small peptides of Staphylococcus aureus with immunosuppressive and antimicrobial properties.
Results: Imaging mass spectrometry (IMS) identified PSM derivatives with properties different from those of the parent forms.
Conclusion:S. aureus generates truncated PSMs with altered antimicrobial and immunostimulatory properties and aureolysin may contribute to processing of some PSMs.
Significance: Observations using the technology of IMS expand our understanding of S. aureus PSMs.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>Bacteria</subject><subject>Bacterial Infections</subject><subject>Bacterial Infections - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Toxins</subject><subject>Bacterial Toxins - chemistry</subject><subject>Erythrocytes - cytology</subject><subject>Hemolysis</subject><subject>Humans</subject><subject>Imaging Mass Spectrometry</subject><subject>Immunosuppressive Agents - pharmacology</subject><subject>Mass Spectrometry (MS)</subject><subject>Mass Spectrometry - methods</subject><subject>Metalloendopeptidases - chemistry</subject><subject>Methicillin-Resistant Staphylococcus aureus - metabolism</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Neutrophils - cytology</subject><subject>Neutrophils - metabolism</subject><subject>Phenol - chemistry</subject><subject>Phenol-soluble Modulins (PSMs)</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sheep</subject><subject>Skin - metabolism</subject><subject>Skin - microbiology</subject><subject>Staphylococcal Skin Infections - microbiology</subject><subject>Staphylococcus aureus</subject><subject>Virulence Factors</subject><subject>Virulence Factors - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNp1kU1v1DAQhi0EokvhzA35yCVbO7Y3yQUJLV8rdQGpPXCzHGeymcqJF9uJtD-Ff4urLRUcmMuMNc-8Hs1LyGvO1pxV8uqutes95-VayKbesCdkxVktCqH4j6dkxVjJi6ZU9QV5EeMdyyEb_pxclKWouGzEivz66hdw9PsAk3dF9G5uHdC972aHE_0AAReTcIFI83Prx3GeMJ0KE6O3aBJ0dA9pQIsu80WAiDGZKdGbZI7DyXnrrZ0jNXOAnHYdTAl7zGNpCH4-DHQ3mgNOB7rPkvTmCDYFP0IKp5fkWW9chFcP-ZLcfvp4u_1SXH_7vNu-vy6slCIVjRW1qVTDhTW1ZbzrW6OY4bJuFeSybvu-6qGXkOtaKSkE75WVJdRclSAuybuz7HFuR-hsXjAYp48BRxNO2hvU_3YmHPTBL1oIyfhmkwXePggE_3OGmPSI0YJzZgI_R80Za3hZNarK6NUZtcHHGKB__IYzfe-nzn7qez_12c888ebv7R75PwZmoDkDkE-0IAQdLcJkocOQb6k7j_8V_w3tRrW-</recordid><startdate>20120420</startdate><enddate>20120420</enddate><creator>Gonzalez, David J.</creator><creator>Okumura, Cheryl Y.</creator><creator>Hollands, Andrew</creator><creator>Kersten, Roland</creator><creator>Akong-Moore, Kathryn</creator><creator>Pence, Morgan A.</creator><creator>Malone, Cheryl L.</creator><creator>Derieux, Jaclyn</creator><creator>Moore, Bradley S.</creator><creator>Horswill, Alexander R.</creator><creator>Dixon, Jack E.</creator><creator>Dorrestein, Pieter C.</creator><creator>Nizet, Victor</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>20120420</creationdate><title>Novel Phenol-soluble Modulin Derivatives in Community-associated Methicillin-resistant Staphylococcus aureus Identified through Imaging Mass Spectrometry</title><author>Gonzalez, David J. ; Okumura, Cheryl Y. ; Hollands, Andrew ; Kersten, Roland ; Akong-Moore, Kathryn ; Pence, Morgan A. ; Malone, Cheryl L. ; Derieux, Jaclyn ; Moore, Bradley S. ; Horswill, Alexander R. ; Dixon, Jack E. ; Dorrestein, Pieter C. ; Nizet, Victor</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-9c38a75913ca8c01dfba50a148b5eba58bff7fef4ea588554331f5c42e8152e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Anti-Infective Agents - pharmacology</topic><topic>Bacteria</topic><topic>Bacterial Infections</topic><topic>Bacterial Infections - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Toxins</topic><topic>Bacterial Toxins - chemistry</topic><topic>Erythrocytes - cytology</topic><topic>Hemolysis</topic><topic>Humans</topic><topic>Imaging Mass Spectrometry</topic><topic>Immunosuppressive Agents - pharmacology</topic><topic>Mass Spectrometry (MS)</topic><topic>Mass Spectrometry - methods</topic><topic>Metalloendopeptidases - chemistry</topic><topic>Methicillin-Resistant Staphylococcus aureus - metabolism</topic><topic>Mice</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Neutrophils - cytology</topic><topic>Neutrophils - metabolism</topic><topic>Phenol - chemistry</topic><topic>Phenol-soluble Modulins (PSMs)</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sheep</topic><topic>Skin - metabolism</topic><topic>Skin - microbiology</topic><topic>Staphylococcal Skin Infections - microbiology</topic><topic>Staphylococcus aureus</topic><topic>Virulence Factors</topic><topic>Virulence Factors - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gonzalez, David J.</creatorcontrib><creatorcontrib>Okumura, Cheryl Y.</creatorcontrib><creatorcontrib>Hollands, Andrew</creatorcontrib><creatorcontrib>Kersten, Roland</creatorcontrib><creatorcontrib>Akong-Moore, Kathryn</creatorcontrib><creatorcontrib>Pence, Morgan A.</creatorcontrib><creatorcontrib>Malone, Cheryl L.</creatorcontrib><creatorcontrib>Derieux, Jaclyn</creatorcontrib><creatorcontrib>Moore, Bradley S.</creatorcontrib><creatorcontrib>Horswill, Alexander R.</creatorcontrib><creatorcontrib>Dixon, Jack E.</creatorcontrib><creatorcontrib>Dorrestein, Pieter C.</creatorcontrib><creatorcontrib>Nizet, Victor</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gonzalez, David J.</au><au>Okumura, Cheryl Y.</au><au>Hollands, Andrew</au><au>Kersten, Roland</au><au>Akong-Moore, Kathryn</au><au>Pence, Morgan A.</au><au>Malone, Cheryl L.</au><au>Derieux, Jaclyn</au><au>Moore, Bradley S.</au><au>Horswill, Alexander R.</au><au>Dixon, Jack E.</au><au>Dorrestein, Pieter C.</au><au>Nizet, Victor</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel Phenol-soluble Modulin Derivatives in Community-associated Methicillin-resistant Staphylococcus aureus Identified through Imaging Mass Spectrometry</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2012-04-20</date><risdate>2012</risdate><volume>287</volume><issue>17</issue><spage>13889</spage><epage>13898</epage><pages>13889-13898</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><notes>Postdoctoral Fellow of the A. P. Giannini Medical Research Foundation.</notes><abstract>Staphylococcus aureus causes a wide range of human disease ranging from localized skin and soft tissue infections to potentially lethal systemic infections. S. aureus has the biosynthetic ability to generate numerous virulence factors that assist in circumventing the innate immune system during disease pathogenesis. Recent studies have uncovered a set of extracellular peptides produced by community-associated methicillin-resistant S. aureus (CA-MRSA) with homology to the phenol-soluble modulins (PSMs) from Staphylococcus epidermidis. CA-MRSA PSMs contribute to skin infection and recruit and lyse neutrophils, and truncated versions of these peptides possess antimicrobial activity. In this study, novel CA-MRSA PSM derivatives were discovered by the use of microbial imaging mass spectrometry. The novel PSM derivatives are compared with their parent full-length peptides for changes in hemolytic, cytolytic, and neutrophil-stimulating activity. A potential contribution of the major S. aureus secreted protease aureolysin in processing PSMs is demonstrated. Finally, we show that PSM processing occurs in multiple CA-MRSA strains by structural confirmation of additional novel derivatives. This work demonstrates that IMS can serve as a useful tool to go beyond genome predictions and expand our understanding of the important family of small peptide virulence factors.
Background: Phenol-soluble modulins (PSMs) are small peptides of Staphylococcus aureus with immunosuppressive and antimicrobial properties.
Results: Imaging mass spectrometry (IMS) identified PSM derivatives with properties different from those of the parent forms.
Conclusion:S. aureus generates truncated PSMs with altered antimicrobial and immunostimulatory properties and aureolysin may contribute to processing of some PSMs.
Significance: Observations using the technology of IMS expand our understanding of S. aureus PSMs.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22371493</pmid><doi>10.1074/jbc.M112.349860</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2012-04, Vol.287 (17), p.13889-13898 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS; Open Access: PubMed Central |
| subjects | Amino Acid Sequence Animals Anti-Infective Agents - pharmacology Bacteria Bacterial Infections Bacterial Infections - metabolism Bacterial Proteins - chemistry Bacterial Toxins Bacterial Toxins - chemistry Erythrocytes - cytology Hemolysis Humans Imaging Mass Spectrometry Immunosuppressive Agents - pharmacology Mass Spectrometry (MS) Mass Spectrometry - methods Metalloendopeptidases - chemistry Methicillin-Resistant Staphylococcus aureus - metabolism Mice Microbiology Molecular Sequence Data Neutrophils - cytology Neutrophils - metabolism Phenol - chemistry Phenol-soluble Modulins (PSMs) Sequence Homology, Amino Acid Sheep Skin - metabolism Skin - microbiology Staphylococcal Skin Infections - microbiology Staphylococcus aureus Virulence Factors Virulence Factors - chemistry |
| title | Novel Phenol-soluble Modulin Derivatives in Community-associated Methicillin-resistant Staphylococcus aureus Identified through Imaging Mass Spectrometry |
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