Surface shaving as a versatile tool to profile global interactions between human serum proteins and the Staphylococcus aureus cell surface
The human commensal bacterium Staphylococcus aureus is renowned as a causative agent of severe invasive diseases. Upon entering the bloodstream, S. aureus can infect almost every tissue and organ system in the human body. To withstand insults from the immune system upon invasion, several immune‐evas...
Gespeichert in:
Veröffentlicht in: | Proteomics (Weinheim) 2011-07, Vol.11 (14), p.2921-2930 |
---|---|
Hauptverfasser: | , , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 2930 |
---|---|
container_issue | 14 |
container_start_page | 2921 |
container_title | Proteomics (Weinheim) |
container_volume | 11 |
creator | Dreisbach, Annette van der Kooi-Pol, Magdalena M. Otto, Andreas Gronau, Katrin Bonarius, Hendrik P. J. Westra, Hans Groen, Herman Becher, Dörte Hecker, Michael van Dijl, Jan M. |
description | The human commensal bacterium Staphylococcus aureus is renowned as a causative agent of severe invasive diseases. Upon entering the bloodstream, S. aureus can infect almost every tissue and organ system in the human body. To withstand insults from the immune system upon invasion, several immune‐evasive mechanisms have evolved in S. aureus, such as complement inhibition by secreted proteins and IgG‐binding by surface‐exposed protein A. While it is generally accepted that S. aureus cells bind a range of host factors for various purposes, no global analyses to profile staphylococcal host factor binding have so far been performed. Therefore, we explored the possibility to profile the binding of human serum proteins to S. aureus cells by “surface shaving” with trypsin and subsequent MS analysis of liberated peptides. This resulted in the identification of several components of the complement system, the platelet factor 4 and the isoform 1 of the inter‐α‐trypsin inhibitor heavy chain H4 on the staphylococcal cell surface. We conclude that surface shaving is a versatile tool to profile global interactions between human serum proteins and the S. aureus cell surface. |
doi_str_mv | 10.1002/pmic.201100134 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_918071973</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3278754521</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5044-568e7bfa0158b6f13ca887eaa1268767d2d2d6d3d6a47e573c8f8ddc7d6868093</originalsourceid><addsrcrecordid>eNqFkU1v1DAQhiMEoqVw5YgsIcQpix3HHzmiFWyLSgEtaCUu1qwz6brkY7GTtvsX-NU4yrIgLitLHo_9zPi13yR5zuiMUZq92TbOzjLKYsJ4_iA5ZZKJtNCSPTysBT9JnoRwExGlC_U4OcmYVLmm-Wnyazn4CiySsIFb114TCATILfoAvauR9F1Xx4lsfVeN-XXdraEmru3Rg-1d1wayxv4OsSWboYGWBPRDM_I9ungIbUn6DZJlD9vNru5sZ-0QtwePMVisaxImCU-TRxXUAZ_t41ny7f27r_Pz9PLT4mL-9jK1guZ5KqRGta6AMqHXsmLcgtYKAVgmtZKqzOKQJS8l5AqF4lZXuiytKqWWmhb8LHk99Y0afw4YetO4MAqBFrshmIJpqlih-FFSa05zrpg6Tqo814xKEcmX_5E33eDb-GDDBFNjOyEjNZso67sQPFZm610DfmcYNaPxZjTeHIyPBS_2bYd1g-UB_-N0BF7tAQgW6spDa134y-WcS6HH3ykm7i7avTtyrfn88WL-r4h0qnWhx_tDLfgfRiquhFldLcyX7x-K5WqxMlf8Nw2M18o</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1517437156</pqid></control><display><type>article</type><title>Surface shaving as a versatile tool to profile global interactions between human serum proteins and the Staphylococcus aureus cell surface</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><creator>Dreisbach, Annette ; van der Kooi-Pol, Magdalena M. ; Otto, Andreas ; Gronau, Katrin ; Bonarius, Hendrik P. J. ; Westra, Hans ; Groen, Herman ; Becher, Dörte ; Hecker, Michael ; van Dijl, Jan M.</creator><creatorcontrib>Dreisbach, Annette ; van der Kooi-Pol, Magdalena M. ; Otto, Andreas ; Gronau, Katrin ; Bonarius, Hendrik P. J. ; Westra, Hans ; Groen, Herman ; Becher, Dörte ; Hecker, Michael ; van Dijl, Jan M.</creatorcontrib><description>The human commensal bacterium Staphylococcus aureus is renowned as a causative agent of severe invasive diseases. Upon entering the bloodstream, S. aureus can infect almost every tissue and organ system in the human body. To withstand insults from the immune system upon invasion, several immune‐evasive mechanisms have evolved in S. aureus, such as complement inhibition by secreted proteins and IgG‐binding by surface‐exposed protein A. While it is generally accepted that S. aureus cells bind a range of host factors for various purposes, no global analyses to profile staphylococcal host factor binding have so far been performed. Therefore, we explored the possibility to profile the binding of human serum proteins to S. aureus cells by “surface shaving” with trypsin and subsequent MS analysis of liberated peptides. This resulted in the identification of several components of the complement system, the platelet factor 4 and the isoform 1 of the inter‐α‐trypsin inhibitor heavy chain H4 on the staphylococcal cell surface. We conclude that surface shaving is a versatile tool to profile global interactions between human serum proteins and the S. aureus cell surface.</description><identifier>ISSN: 1615-9853</identifier><identifier>ISSN: 1615-9861</identifier><identifier>ISSN: 1862-8346</identifier><identifier>EISSN: 1615-9861</identifier><identifier>DOI: 10.1002/pmic.201100134</identifier><identifier>PMID: 21674804</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Alpha-Globulins - chemistry ; Alpha-Globulins - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Blood Proteins - chemistry ; Blood Proteins - metabolism ; Cell Membrane - chemistry ; Complement ; Fundamental and applied biological sciences. Psychology ; Genes ; Host-pathogen interaction ; Humans ; Immune system ; Immunoglobulin G - chemistry ; Mass Spectrometry - methods ; Microbiology ; Miscellaneous ; Newman ; Peptides ; Peptides - analysis ; Protein Binding ; Proteins ; Staphylococcal Infections - metabolism ; Staphylococcus ; Staphylococcus aureus ; Staphylococcus aureus - chemistry ; Staphylococcus aureus - cytology ; Surface Properties ; Trypsin - metabolism ; USA300</subject><ispartof>Proteomics (Weinheim), 2011-07, Vol.11 (14), p.2921-2930</ispartof><rights>Copyright © 2011 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5044-568e7bfa0158b6f13ca887eaa1268767d2d2d6d3d6a47e573c8f8ddc7d6868093</citedby><cites>FETCH-LOGICAL-c5044-568e7bfa0158b6f13ca887eaa1268767d2d2d6d3d6a47e573c8f8ddc7d6868093</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fpmic.201100134$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fpmic.201100134$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24336589$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21674804$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dreisbach, Annette</creatorcontrib><creatorcontrib>van der Kooi-Pol, Magdalena M.</creatorcontrib><creatorcontrib>Otto, Andreas</creatorcontrib><creatorcontrib>Gronau, Katrin</creatorcontrib><creatorcontrib>Bonarius, Hendrik P. J.</creatorcontrib><creatorcontrib>Westra, Hans</creatorcontrib><creatorcontrib>Groen, Herman</creatorcontrib><creatorcontrib>Becher, Dörte</creatorcontrib><creatorcontrib>Hecker, Michael</creatorcontrib><creatorcontrib>van Dijl, Jan M.</creatorcontrib><title>Surface shaving as a versatile tool to profile global interactions between human serum proteins and the Staphylococcus aureus cell surface</title><title>Proteomics (Weinheim)</title><addtitle>Proteomics</addtitle><description>The human commensal bacterium Staphylococcus aureus is renowned as a causative agent of severe invasive diseases. Upon entering the bloodstream, S. aureus can infect almost every tissue and organ system in the human body. To withstand insults from the immune system upon invasion, several immune‐evasive mechanisms have evolved in S. aureus, such as complement inhibition by secreted proteins and IgG‐binding by surface‐exposed protein A. While it is generally accepted that S. aureus cells bind a range of host factors for various purposes, no global analyses to profile staphylococcal host factor binding have so far been performed. Therefore, we explored the possibility to profile the binding of human serum proteins to S. aureus cells by “surface shaving” with trypsin and subsequent MS analysis of liberated peptides. This resulted in the identification of several components of the complement system, the platelet factor 4 and the isoform 1 of the inter‐α‐trypsin inhibitor heavy chain H4 on the staphylococcal cell surface. We conclude that surface shaving is a versatile tool to profile global interactions between human serum proteins and the S. aureus cell surface.</description><subject>Alpha-Globulins - chemistry</subject><subject>Alpha-Globulins - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - chemistry</subject><subject>Blood Proteins - metabolism</subject><subject>Cell Membrane - chemistry</subject><subject>Complement</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Host-pathogen interaction</subject><subject>Humans</subject><subject>Immune system</subject><subject>Immunoglobulin G - chemistry</subject><subject>Mass Spectrometry - methods</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Newman</subject><subject>Peptides</subject><subject>Peptides - analysis</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Staphylococcal Infections - metabolism</subject><subject>Staphylococcus</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus aureus - chemistry</subject><subject>Staphylococcus aureus - cytology</subject><subject>Surface Properties</subject><subject>Trypsin - metabolism</subject><subject>USA300</subject><issn>1615-9853</issn><issn>1615-9861</issn><issn>1862-8346</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhiMEoqVw5YgsIcQpix3HHzmiFWyLSgEtaCUu1qwz6brkY7GTtvsX-NU4yrIgLitLHo_9zPi13yR5zuiMUZq92TbOzjLKYsJ4_iA5ZZKJtNCSPTysBT9JnoRwExGlC_U4OcmYVLmm-Wnyazn4CiySsIFb114TCATILfoAvauR9F1Xx4lsfVeN-XXdraEmru3Rg-1d1wayxv4OsSWboYGWBPRDM_I9ungIbUn6DZJlD9vNru5sZ-0QtwePMVisaxImCU-TRxXUAZ_t41ny7f27r_Pz9PLT4mL-9jK1guZ5KqRGta6AMqHXsmLcgtYKAVgmtZKqzOKQJS8l5AqF4lZXuiytKqWWmhb8LHk99Y0afw4YetO4MAqBFrshmIJpqlih-FFSa05zrpg6Tqo814xKEcmX_5E33eDb-GDDBFNjOyEjNZso67sQPFZm610DfmcYNaPxZjTeHIyPBS_2bYd1g-UB_-N0BF7tAQgW6spDa134y-WcS6HH3ykm7i7avTtyrfn88WL-r4h0qnWhx_tDLfgfRiquhFldLcyX7x-K5WqxMlf8Nw2M18o</recordid><startdate>20110701</startdate><enddate>20110701</enddate><creator>Dreisbach, Annette</creator><creator>van der Kooi-Pol, Magdalena M.</creator><creator>Otto, Andreas</creator><creator>Gronau, Katrin</creator><creator>Bonarius, Hendrik P. J.</creator><creator>Westra, Hans</creator><creator>Groen, Herman</creator><creator>Becher, Dörte</creator><creator>Hecker, Michael</creator><creator>van Dijl, Jan M.</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley-VCH</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</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>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>20110701</creationdate><title>Surface shaving as a versatile tool to profile global interactions between human serum proteins and the Staphylococcus aureus cell surface</title><author>Dreisbach, Annette ; van der Kooi-Pol, Magdalena M. ; Otto, Andreas ; Gronau, Katrin ; Bonarius, Hendrik P. J. ; Westra, Hans ; Groen, Herman ; Becher, Dörte ; Hecker, Michael ; van Dijl, Jan M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5044-568e7bfa0158b6f13ca887eaa1268767d2d2d6d3d6a47e573c8f8ddc7d6868093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Alpha-Globulins - chemistry</topic><topic>Alpha-Globulins - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - chemistry</topic><topic>Blood Proteins - metabolism</topic><topic>Cell Membrane - chemistry</topic><topic>Complement</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes</topic><topic>Host-pathogen interaction</topic><topic>Humans</topic><topic>Immune system</topic><topic>Immunoglobulin G - chemistry</topic><topic>Mass Spectrometry - methods</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Newman</topic><topic>Peptides</topic><topic>Peptides - analysis</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Staphylococcal Infections - metabolism</topic><topic>Staphylococcus</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus aureus - chemistry</topic><topic>Staphylococcus aureus - cytology</topic><topic>Surface Properties</topic><topic>Trypsin - metabolism</topic><topic>USA300</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dreisbach, Annette</creatorcontrib><creatorcontrib>van der Kooi-Pol, Magdalena M.</creatorcontrib><creatorcontrib>Otto, Andreas</creatorcontrib><creatorcontrib>Gronau, Katrin</creatorcontrib><creatorcontrib>Bonarius, Hendrik P. J.</creatorcontrib><creatorcontrib>Westra, Hans</creatorcontrib><creatorcontrib>Groen, Herman</creatorcontrib><creatorcontrib>Becher, Dörte</creatorcontrib><creatorcontrib>Hecker, Michael</creatorcontrib><creatorcontrib>van Dijl, Jan M.</creatorcontrib><collection>Istex</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>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Proteomics (Weinheim)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dreisbach, Annette</au><au>van der Kooi-Pol, Magdalena M.</au><au>Otto, Andreas</au><au>Gronau, Katrin</au><au>Bonarius, Hendrik P. J.</au><au>Westra, Hans</au><au>Groen, Herman</au><au>Becher, Dörte</au><au>Hecker, Michael</au><au>van Dijl, Jan M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Surface shaving as a versatile tool to profile global interactions between human serum proteins and the Staphylococcus aureus cell surface</atitle><jtitle>Proteomics (Weinheim)</jtitle><addtitle>Proteomics</addtitle><date>2011-07-01</date><risdate>2011</risdate><volume>11</volume><issue>14</issue><spage>2921</spage><epage>2930</epage><pages>2921-2930</pages><issn>1615-9853</issn><issn>1615-9861</issn><issn>1862-8346</issn><eissn>1615-9861</eissn><abstract>The human commensal bacterium Staphylococcus aureus is renowned as a causative agent of severe invasive diseases. Upon entering the bloodstream, S. aureus can infect almost every tissue and organ system in the human body. To withstand insults from the immune system upon invasion, several immune‐evasive mechanisms have evolved in S. aureus, such as complement inhibition by secreted proteins and IgG‐binding by surface‐exposed protein A. While it is generally accepted that S. aureus cells bind a range of host factors for various purposes, no global analyses to profile staphylococcal host factor binding have so far been performed. Therefore, we explored the possibility to profile the binding of human serum proteins to S. aureus cells by “surface shaving” with trypsin and subsequent MS analysis of liberated peptides. This resulted in the identification of several components of the complement system, the platelet factor 4 and the isoform 1 of the inter‐α‐trypsin inhibitor heavy chain H4 on the staphylococcal cell surface. We conclude that surface shaving is a versatile tool to profile global interactions between human serum proteins and the S. aureus cell surface.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>21674804</pmid><doi>10.1002/pmic.201100134</doi><tpages>10</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1615-9853 |
ispartof | Proteomics (Weinheim), 2011-07, Vol.11 (14), p.2921-2930 |
issn | 1615-9853 1615-9861 1862-8346 1615-9861 |
language | eng |
recordid | cdi_proquest_miscellaneous_918071973 |
source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
subjects | Alpha-Globulins - chemistry Alpha-Globulins - metabolism Analytical, structural and metabolic biochemistry Animals Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Blood Proteins - chemistry Blood Proteins - metabolism Cell Membrane - chemistry Complement Fundamental and applied biological sciences. Psychology Genes Host-pathogen interaction Humans Immune system Immunoglobulin G - chemistry Mass Spectrometry - methods Microbiology Miscellaneous Newman Peptides Peptides - analysis Protein Binding Proteins Staphylococcal Infections - metabolism Staphylococcus Staphylococcus aureus Staphylococcus aureus - chemistry Staphylococcus aureus - cytology Surface Properties Trypsin - metabolism USA300 |
title | Surface shaving as a versatile tool to profile global interactions between human serum proteins and the Staphylococcus aureus cell surface |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T07%3A42%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Surface%20shaving%20as%20a%20versatile%20tool%20to%20profile%20global%20interactions%20between%20human%20serum%20proteins%20and%20the%20Staphylococcus%20aureus%20cell%20surface&rft.jtitle=Proteomics%20(Weinheim)&rft.au=Dreisbach,%20Annette&rft.date=2011-07-01&rft.volume=11&rft.issue=14&rft.spage=2921&rft.epage=2930&rft.pages=2921-2930&rft.issn=1615-9853&rft.eissn=1615-9861&rft_id=info:doi/10.1002/pmic.201100134&rft_dat=%3Cproquest_cross%3E3278754521%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1517437156&rft_id=info:pmid/21674804&rfr_iscdi=true |