Covalent attachment and Pro‐Pro endopeptidase (PPEP‐1)‐mediated release of Clostridium difficile cell surface proteins involved in adhesion
Summary In the past decade, Clostridium difficile has emerged as an important gut pathogen. This anaerobic, Gram‐positive bacterium is the main cause of infectious nosocomial diarrhea. Whereas much is known about the mechanism through which the C. difficile toxins cause diarrhea, relatively little i...
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| Veröffentlicht in: | Molecular microbiology 2017-09, Vol.105 (5), p.663-673 |
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| creator | Corver, Jeroen Cordo’, Valentina van Leeuwen, Hans C. Klychnikov, Oleg I. Hensbergen, Paul J. |
| description | Summary
In the past decade, Clostridium difficile has emerged as an important gut pathogen. This anaerobic, Gram‐positive bacterium is the main cause of infectious nosocomial diarrhea. Whereas much is known about the mechanism through which the C. difficile toxins cause diarrhea, relatively little is known about the dynamics of adhesion and motility, which is mediated by cell surface proteins. This review will discuss the recent advances in our understanding of the sortase‐mediated covalent attachment of cell surface (adhesion) proteins to the peptidoglycan layer of C. difficile and their release through the action of a highly specific secreted metalloprotease (Pro‐Pro endopeptidase 1, PPEP‐1). Specific emphasis will be on a model in which PPEP‐1 and its substrates control the switch from a sessile to motile phenotype in C. difficile, and how this is regulated by the cyclic dinucleotide c‐di‐GMP (3′‐5′ cyclic dimeric guanosine monophosphate).
Two C. difficile LPxTG‐like proteins (CD2831 and CD3246), involved in adhesion, are covalently attached to the peptidoglycan layer via a sortase‐mediated reaction. Release of these proteins is mediated by the activity of a highly specific secreted C. difficile protease, Pro‐Pro endopeptidase 1 (PPEP‐1), suggesting a role for this protease in the switch from a sessile to motile lifestyle in C. difficile |
| doi_str_mv | 10.1111/mmi.13736 |
| format | Article |
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In the past decade, Clostridium difficile has emerged as an important gut pathogen. This anaerobic, Gram‐positive bacterium is the main cause of infectious nosocomial diarrhea. Whereas much is known about the mechanism through which the C. difficile toxins cause diarrhea, relatively little is known about the dynamics of adhesion and motility, which is mediated by cell surface proteins. This review will discuss the recent advances in our understanding of the sortase‐mediated covalent attachment of cell surface (adhesion) proteins to the peptidoglycan layer of C. difficile and their release through the action of a highly specific secreted metalloprotease (Pro‐Pro endopeptidase 1, PPEP‐1). Specific emphasis will be on a model in which PPEP‐1 and its substrates control the switch from a sessile to motile phenotype in C. difficile, and how this is regulated by the cyclic dinucleotide c‐di‐GMP (3′‐5′ cyclic dimeric guanosine monophosphate).
Two C. difficile LPxTG‐like proteins (CD2831 and CD3246), involved in adhesion, are covalently attached to the peptidoglycan layer via a sortase‐mediated reaction. Release of these proteins is mediated by the activity of a highly specific secreted C. difficile protease, Pro‐Pro endopeptidase 1 (PPEP‐1), suggesting a role for this protease in the switch from a sessile to motile lifestyle in C. difficile</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/mmi.13736</identifier><identifier>PMID: 28636257</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Adhesion ; Bacterial Proteins - metabolism ; Beryllium ; Biofilms ; Cell Adhesion - physiology ; Cell surface ; Clostridium difficile - metabolism ; Covalence ; Cross Infection ; Cyclic GMP - analogs & derivatives ; Cyclic GMP - metabolism ; Diarrhea ; Dipeptides ; Endopeptidase ; Endopeptidases - metabolism ; Gene Expression Regulation, Bacterial - genetics ; Guanosine ; Hospitals ; Humans ; Membrane Proteins - metabolism ; Metalloproteases - metabolism ; Metalloproteinase ; Nosocomial infection ; Peptidoglycan - metabolism ; Peptidoglycans ; Proteins ; Sortase ; Substrates ; Toxins</subject><ispartof>Molecular microbiology, 2017-09, Vol.105 (5), p.663-673</ispartof><rights>2017 John Wiley & Sons Ltd</rights><rights>2017 John Wiley & Sons Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3886-1e8b3368dfcd58f28e555c91163284a500fb65437c1398a80044548361f8f6693</citedby><cites>FETCH-LOGICAL-c3886-1e8b3368dfcd58f28e555c91163284a500fb65437c1398a80044548361f8f6693</cites><orcidid>0000-0002-3193-5445</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fmmi.13736$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fmmi.13736$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28636257$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Corver, Jeroen</creatorcontrib><creatorcontrib>Cordo’, Valentina</creatorcontrib><creatorcontrib>van Leeuwen, Hans C.</creatorcontrib><creatorcontrib>Klychnikov, Oleg I.</creatorcontrib><creatorcontrib>Hensbergen, Paul J.</creatorcontrib><title>Covalent attachment and Pro‐Pro endopeptidase (PPEP‐1)‐mediated release of Clostridium difficile cell surface proteins involved in adhesion</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
In the past decade, Clostridium difficile has emerged as an important gut pathogen. This anaerobic, Gram‐positive bacterium is the main cause of infectious nosocomial diarrhea. Whereas much is known about the mechanism through which the C. difficile toxins cause diarrhea, relatively little is known about the dynamics of adhesion and motility, which is mediated by cell surface proteins. This review will discuss the recent advances in our understanding of the sortase‐mediated covalent attachment of cell surface (adhesion) proteins to the peptidoglycan layer of C. difficile and their release through the action of a highly specific secreted metalloprotease (Pro‐Pro endopeptidase 1, PPEP‐1). Specific emphasis will be on a model in which PPEP‐1 and its substrates control the switch from a sessile to motile phenotype in C. difficile, and how this is regulated by the cyclic dinucleotide c‐di‐GMP (3′‐5′ cyclic dimeric guanosine monophosphate).
Two C. difficile LPxTG‐like proteins (CD2831 and CD3246), involved in adhesion, are covalently attached to the peptidoglycan layer via a sortase‐mediated reaction. Release of these proteins is mediated by the activity of a highly specific secreted C. difficile protease, Pro‐Pro endopeptidase 1 (PPEP‐1), suggesting a role for this protease in the switch from a sessile to motile lifestyle in C. difficile</description><subject>Adhesion</subject><subject>Bacterial Proteins - metabolism</subject><subject>Beryllium</subject><subject>Biofilms</subject><subject>Cell Adhesion - physiology</subject><subject>Cell surface</subject><subject>Clostridium difficile - metabolism</subject><subject>Covalence</subject><subject>Cross Infection</subject><subject>Cyclic GMP - analogs & derivatives</subject><subject>Cyclic GMP - metabolism</subject><subject>Diarrhea</subject><subject>Dipeptides</subject><subject>Endopeptidase</subject><subject>Endopeptidases - metabolism</subject><subject>Gene Expression Regulation, Bacterial - genetics</subject><subject>Guanosine</subject><subject>Hospitals</subject><subject>Humans</subject><subject>Membrane Proteins - metabolism</subject><subject>Metalloproteases - metabolism</subject><subject>Metalloproteinase</subject><subject>Nosocomial infection</subject><subject>Peptidoglycan - metabolism</subject><subject>Peptidoglycans</subject><subject>Proteins</subject><subject>Sortase</subject><subject>Substrates</subject><subject>Toxins</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kbFuFDEQhi0EIkeg4AWQJZqk2MT2rH3eEp0CRErEFSDRrXz2WHG0ax_27kXpeAR4RZ4EXy5QIOFiPNJ88-vX_IS85uyM13c-juGMwxLUE7LgoGQjOqmfkgXrJGtAi69H5EUpt4xxYAqekyOhFSghlwvyc5V2ZsA4UTNNxt6MD210dJ3Tr-8_aqUYXdridgrOFKQn6_XFuk74aS0jumAmdDTjgPtp8nQ1pDLl4MI8Uhe8DzYMSC0OAy1z9sYi3eY0YYiFhrhLw67uh0iNu8ESUnxJnnkzFHz1-B-TL-8vPq8-NlefPlyu3l01FrRWDUe9AVDaeeuk9kKjlNJ2nCsQujWSMb9RsoWl5dBpoxlrW9lqUNxrr1QHx-TkoFvdfJuxTP0Yyt6miZjm0vOOC96JVkBF3_6D3qY5x-quUsBboZYgK3V6oGxOpWT0_TaH0eT7nrN-n1Nfc-ofcqrsm0fFeVOP-Jf8E0wFzg_AXb3e_f-V-uvry4PkbwWNnyY</recordid><startdate>201709</startdate><enddate>201709</enddate><creator>Corver, Jeroen</creator><creator>Cordo’, Valentina</creator><creator>van Leeuwen, Hans C.</creator><creator>Klychnikov, Oleg I.</creator><creator>Hensbergen, Paul J.</creator><general>Blackwell Publishing Ltd</general><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3193-5445</orcidid></search><sort><creationdate>201709</creationdate><title>Covalent attachment and Pro‐Pro endopeptidase (PPEP‐1)‐mediated release of Clostridium difficile cell surface proteins involved in adhesion</title><author>Corver, Jeroen ; Cordo’, Valentina ; van Leeuwen, Hans C. ; Klychnikov, Oleg I. ; Hensbergen, Paul J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3886-1e8b3368dfcd58f28e555c91163284a500fb65437c1398a80044548361f8f6693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Adhesion</topic><topic>Bacterial Proteins - metabolism</topic><topic>Beryllium</topic><topic>Biofilms</topic><topic>Cell Adhesion - physiology</topic><topic>Cell surface</topic><topic>Clostridium difficile - metabolism</topic><topic>Covalence</topic><topic>Cross Infection</topic><topic>Cyclic GMP - analogs & derivatives</topic><topic>Cyclic GMP - metabolism</topic><topic>Diarrhea</topic><topic>Dipeptides</topic><topic>Endopeptidase</topic><topic>Endopeptidases - metabolism</topic><topic>Gene Expression Regulation, Bacterial - genetics</topic><topic>Guanosine</topic><topic>Hospitals</topic><topic>Humans</topic><topic>Membrane Proteins - metabolism</topic><topic>Metalloproteases - metabolism</topic><topic>Metalloproteinase</topic><topic>Nosocomial infection</topic><topic>Peptidoglycan - metabolism</topic><topic>Peptidoglycans</topic><topic>Proteins</topic><topic>Sortase</topic><topic>Substrates</topic><topic>Toxins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Corver, Jeroen</creatorcontrib><creatorcontrib>Cordo’, Valentina</creatorcontrib><creatorcontrib>van Leeuwen, Hans C.</creatorcontrib><creatorcontrib>Klychnikov, Oleg I.</creatorcontrib><creatorcontrib>Hensbergen, Paul J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Corver, Jeroen</au><au>Cordo’, Valentina</au><au>van Leeuwen, Hans C.</au><au>Klychnikov, Oleg I.</au><au>Hensbergen, Paul J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Covalent attachment and Pro‐Pro endopeptidase (PPEP‐1)‐mediated release of Clostridium difficile cell surface proteins involved in adhesion</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2017-09</date><risdate>2017</risdate><volume>105</volume><issue>5</issue><spage>663</spage><epage>673</epage><pages>663-673</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
In the past decade, Clostridium difficile has emerged as an important gut pathogen. This anaerobic, Gram‐positive bacterium is the main cause of infectious nosocomial diarrhea. Whereas much is known about the mechanism through which the C. difficile toxins cause diarrhea, relatively little is known about the dynamics of adhesion and motility, which is mediated by cell surface proteins. This review will discuss the recent advances in our understanding of the sortase‐mediated covalent attachment of cell surface (adhesion) proteins to the peptidoglycan layer of C. difficile and their release through the action of a highly specific secreted metalloprotease (Pro‐Pro endopeptidase 1, PPEP‐1). Specific emphasis will be on a model in which PPEP‐1 and its substrates control the switch from a sessile to motile phenotype in C. difficile, and how this is regulated by the cyclic dinucleotide c‐di‐GMP (3′‐5′ cyclic dimeric guanosine monophosphate).
Two C. difficile LPxTG‐like proteins (CD2831 and CD3246), involved in adhesion, are covalently attached to the peptidoglycan layer via a sortase‐mediated reaction. Release of these proteins is mediated by the activity of a highly specific secreted C. difficile protease, Pro‐Pro endopeptidase 1 (PPEP‐1), suggesting a role for this protease in the switch from a sessile to motile lifestyle in C. difficile</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>28636257</pmid><doi>10.1111/mmi.13736</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-3193-5445</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adhesion Bacterial Proteins - metabolism Beryllium Biofilms Cell Adhesion - physiology Cell surface Clostridium difficile - metabolism Covalence Cross Infection Cyclic GMP - analogs & derivatives Cyclic GMP - metabolism Diarrhea Dipeptides Endopeptidase Endopeptidases - metabolism Gene Expression Regulation, Bacterial - genetics Guanosine Hospitals Humans Membrane Proteins - metabolism Metalloproteases - metabolism Metalloproteinase Nosocomial infection Peptidoglycan - metabolism Peptidoglycans Proteins Sortase Substrates Toxins |
| title | Covalent attachment and Pro‐Pro endopeptidase (PPEP‐1)‐mediated release of Clostridium difficile cell surface proteins involved in adhesion |
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