Phylogeny of the Staphylococcal Major Autolysin and Its Use in Genus and Species Typing
The major staphylococcal autolysin Atl is an important player in cell separation and daughter cell formation. In this study, we investigated the amino acid sequences of Atl proteins derived from 15 staphylococcal and 1 macrococcal species representatives. The overall organization of the bifunctional...
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| Veröffentlicht in: | Journal of Bacteriology 2012-05, Vol.194 (10), p.2630-2636 |
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| creator | Albrecht, Till Raue, Stefan Rosenstein, Ralf Nieselt, Kay Götz, Friedrich |
| description | The major staphylococcal autolysin Atl is an important player in cell separation and daughter cell formation. In this study, we investigated the amino acid sequences of Atl proteins derived from 15 staphylococcal and 1 macrococcal species representatives. The overall organization of the bifunctional precursor protein consisting of the signal peptide, a propeptide (PP), the amidase (AM), six repeat sequences (R1 to R6), and the glucosaminidase (GL) was highly conserved in all of the species. The most-conserved domains were the enzyme domains AM and GL; the least-conserved regions were the PP and R regions. An Atl-based phylogenetic tree for the various species representatives correlated well with the corresponding 16S rRNA-based tree and also perfectly matched the phylogenetic trees based on core genome analysis. The phylogenetic distance analysis of 18 AtlA proteins of various Staphylococcus aureus strains and 15 AtlE proteins of S. epidermidis revealed that both species representatives formed a relatively homogeneous cluster. Two S. epidermidis strains, M23864:W1 and VCU116, were identified by Atl typing that clustered far more distantly and belonged to either S. caprae and S. capitis or a new subspecies. Here we show that Atl typing is a useful tool for staphylococcal genus and species typing by using either the highly conserved AM domain or the less-conserved PP domain. |
| doi_str_mv | 10.1128/JB.06609-11 |
| format | Article |
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In this study, we investigated the amino acid sequences of Atl proteins derived from 15 staphylococcal and 1 macrococcal species representatives. The overall organization of the bifunctional precursor protein consisting of the signal peptide, a propeptide (PP), the amidase (AM), six repeat sequences (R1 to R6), and the glucosaminidase (GL) was highly conserved in all of the species. The most-conserved domains were the enzyme domains AM and GL; the least-conserved regions were the PP and R regions. An Atl-based phylogenetic tree for the various species representatives correlated well with the corresponding 16S rRNA-based tree and also perfectly matched the phylogenetic trees based on core genome analysis. The phylogenetic distance analysis of 18 AtlA proteins of various Staphylococcus aureus strains and 15 AtlE proteins of S. epidermidis revealed that both species representatives formed a relatively homogeneous cluster. Two S. epidermidis strains, M23864:W1 and VCU116, were identified by Atl typing that clustered far more distantly and belonged to either S. caprae and S. capitis or a new subspecies. Here we show that Atl typing is a useful tool for staphylococcal genus and species typing by using either the highly conserved AM domain or the less-conserved PP domain.</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>EISSN: 1067-8832</identifier><identifier>DOI: 10.1128/JB.06609-11</identifier><identifier>PMID: 22427631</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>amidase ; Amino acids ; Bacteriology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; gametolysin ; Gene Expression Regulation, Bacterial - physiology ; Gene Expression Regulation, Enzymologic - physiology ; Genome, Bacterial ; Microbiology ; Miscellaneous ; N-Acetylmuramoyl-L-alanine Amidase - genetics ; N-Acetylmuramoyl-L-alanine Amidase - metabolism ; new subspecies ; Peptides ; Phylogenetics ; Phylogeny ; Protein Structure, Tertiary ; Proteins ; RNA, Ribosomal, 16S - genetics ; RNA, Ribosomal, 16S - metabolism ; sequence analysis ; signal peptide ; Species Specificity ; Staphylococcus - classification ; Staphylococcus - enzymology ; Staphylococcus aureus ; Staphylococcus infections ; trees</subject><ispartof>Journal of Bacteriology, 2012-05, Vol.194 (10), p.2630-2636</ispartof><rights>2015 INIST-CNRS</rights><rights>Copyright American Society for Microbiology May 2012</rights><rights>Copyright © 2012, American Society for Microbiology. All Rights Reserved. 2012 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c598t-46aa99e5828a88f9cbb70686fd0a850e1b9f4502a510cf5f04c84f095889f1333</citedby><cites>FETCH-LOGICAL-c598t-46aa99e5828a88f9cbb70686fd0a850e1b9f4502a510cf5f04c84f095889f1333</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/PMC3347219/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347219/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25872040$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22427631$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Albrecht, Till</creatorcontrib><creatorcontrib>Raue, Stefan</creatorcontrib><creatorcontrib>Rosenstein, Ralf</creatorcontrib><creatorcontrib>Nieselt, Kay</creatorcontrib><creatorcontrib>Götz, Friedrich</creatorcontrib><title>Phylogeny of the Staphylococcal Major Autolysin and Its Use in Genus and Species Typing</title><title>Journal of Bacteriology</title><addtitle>J Bacteriol</addtitle><description>The major staphylococcal autolysin Atl is an important player in cell separation and daughter cell formation. In this study, we investigated the amino acid sequences of Atl proteins derived from 15 staphylococcal and 1 macrococcal species representatives. The overall organization of the bifunctional precursor protein consisting of the signal peptide, a propeptide (PP), the amidase (AM), six repeat sequences (R1 to R6), and the glucosaminidase (GL) was highly conserved in all of the species. The most-conserved domains were the enzyme domains AM and GL; the least-conserved regions were the PP and R regions. An Atl-based phylogenetic tree for the various species representatives correlated well with the corresponding 16S rRNA-based tree and also perfectly matched the phylogenetic trees based on core genome analysis. The phylogenetic distance analysis of 18 AtlA proteins of various Staphylococcus aureus strains and 15 AtlE proteins of S. epidermidis revealed that both species representatives formed a relatively homogeneous cluster. Two S. epidermidis strains, M23864:W1 and VCU116, were identified by Atl typing that clustered far more distantly and belonged to either S. caprae and S. capitis or a new subspecies. Here we show that Atl typing is a useful tool for staphylococcal genus and species typing by using either the highly conserved AM domain or the less-conserved PP domain.</description><subject>amidase</subject><subject>Amino acids</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gametolysin</subject><subject>Gene Expression Regulation, Bacterial - physiology</subject><subject>Gene Expression Regulation, Enzymologic - physiology</subject><subject>Genome, Bacterial</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>N-Acetylmuramoyl-L-alanine Amidase - genetics</subject><subject>N-Acetylmuramoyl-L-alanine Amidase - metabolism</subject><subject>new subspecies</subject><subject>Peptides</subject><subject>Phylogenetics</subject><subject>Phylogeny</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>RNA, Ribosomal, 16S - genetics</subject><subject>RNA, Ribosomal, 16S - metabolism</subject><subject>sequence analysis</subject><subject>signal peptide</subject><subject>Species Specificity</subject><subject>Staphylococcus - classification</subject><subject>Staphylococcus - enzymology</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus infections</subject><subject>trees</subject><issn>0021-9193</issn><issn>1098-5530</issn><issn>1067-8832</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0s2L1DAUAPAgijuOnrxrWREE6fry1SYXYXfRdZcVhdnBY0gzSadDp6lJq_S_t92O68dpDyHk5ccL770g9BzDCcZEvLs6O4EsA5li_AAtMEiRck7hIVoAEJxKLOkRehLjDgAzxsljdEQII3lG8QJ9-7odal_aZki8S7qtTVadbqeY8cboOvmsdz4kp33n6yFWTaKbTXLZxWQdbTIeL2zTx9vgqrWmsjG5GdqqKZ-iR07X0T477Eu0_vjh5vxTev3l4vL89Do1XIouZZnWUlouiNBCOGmKIodMZG4DWnCwuJCOcSCaYzCOO2BGMAeSCyEdppQu0fs5b9sXe7sxtumCrlUbqr0Og_K6Uv_eNNVWlf6HopTlZGzNEr05JAj-e29jp_ZVNLaudWN9HxUGnMuc0ZzflxIM96FAKJMMj_TVf3Tn-9CMTZtVBtlIl-jtrEzwMQbr7krEoKZvoK7O1O03GE-jfvF3V-7s77mP4PUB6DhO2QXdmCr-cVzkBNhUx_HstlW5_VkFq3Tcq12hsGTTyySjE3o5I6e90mUYE61XBDCHaREp6C9dAsvE</recordid><startdate>20120501</startdate><enddate>20120501</enddate><creator>Albrecht, Till</creator><creator>Raue, Stefan</creator><creator>Rosenstein, Ralf</creator><creator>Nieselt, Kay</creator><creator>Götz, Friedrich</creator><general>American Society for Microbiology</general><scope>FBQ</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>7QL</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><scope>5PM</scope></search><sort><creationdate>20120501</creationdate><title>Phylogeny of the Staphylococcal Major Autolysin and Its Use in Genus and Species Typing</title><author>Albrecht, Till ; Raue, Stefan ; Rosenstein, Ralf ; Nieselt, Kay ; Götz, Friedrich</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c598t-46aa99e5828a88f9cbb70686fd0a850e1b9f4502a510cf5f04c84f095889f1333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>amidase</topic><topic>Amino acids</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gametolysin</topic><topic>Gene Expression Regulation, Bacterial - physiology</topic><topic>Gene Expression Regulation, Enzymologic - physiology</topic><topic>Genome, Bacterial</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>N-Acetylmuramoyl-L-alanine Amidase - genetics</topic><topic>N-Acetylmuramoyl-L-alanine Amidase - metabolism</topic><topic>new subspecies</topic><topic>Peptides</topic><topic>Phylogenetics</topic><topic>Phylogeny</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>RNA, Ribosomal, 16S - genetics</topic><topic>RNA, Ribosomal, 16S - metabolism</topic><topic>sequence analysis</topic><topic>signal peptide</topic><topic>Species Specificity</topic><topic>Staphylococcus - classification</topic><topic>Staphylococcus - enzymology</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus infections</topic><topic>trees</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Albrecht, Till</creatorcontrib><creatorcontrib>Raue, Stefan</creatorcontrib><creatorcontrib>Rosenstein, Ralf</creatorcontrib><creatorcontrib>Nieselt, Kay</creatorcontrib><creatorcontrib>Götz, Friedrich</creatorcontrib><collection>AGRIS</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>Bacteriology Abstracts (Microbiology B)</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Albrecht, Till</au><au>Raue, Stefan</au><au>Rosenstein, Ralf</au><au>Nieselt, Kay</au><au>Götz, Friedrich</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phylogeny of the Staphylococcal Major Autolysin and Its Use in Genus and Species Typing</atitle><jtitle>Journal of Bacteriology</jtitle><addtitle>J Bacteriol</addtitle><date>2012-05-01</date><risdate>2012</risdate><volume>194</volume><issue>10</issue><spage>2630</spage><epage>2636</epage><pages>2630-2636</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><eissn>1067-8832</eissn><coden>JOBAAY</coden><abstract>The major staphylococcal autolysin Atl is an important player in cell separation and daughter cell formation. In this study, we investigated the amino acid sequences of Atl proteins derived from 15 staphylococcal and 1 macrococcal species representatives. The overall organization of the bifunctional precursor protein consisting of the signal peptide, a propeptide (PP), the amidase (AM), six repeat sequences (R1 to R6), and the glucosaminidase (GL) was highly conserved in all of the species. The most-conserved domains were the enzyme domains AM and GL; the least-conserved regions were the PP and R regions. An Atl-based phylogenetic tree for the various species representatives correlated well with the corresponding 16S rRNA-based tree and also perfectly matched the phylogenetic trees based on core genome analysis. The phylogenetic distance analysis of 18 AtlA proteins of various Staphylococcus aureus strains and 15 AtlE proteins of S. epidermidis revealed that both species representatives formed a relatively homogeneous cluster. Two S. epidermidis strains, M23864:W1 and VCU116, were identified by Atl typing that clustered far more distantly and belonged to either S. caprae and S. capitis or a new subspecies. Here we show that Atl typing is a useful tool for staphylococcal genus and species typing by using either the highly conserved AM domain or the less-conserved PP domain.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>22427631</pmid><doi>10.1128/JB.06609-11</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | amidase Amino acids Bacteriology Biological and medical sciences Fundamental and applied biological sciences. Psychology gametolysin Gene Expression Regulation, Bacterial - physiology Gene Expression Regulation, Enzymologic - physiology Genome, Bacterial Microbiology Miscellaneous N-Acetylmuramoyl-L-alanine Amidase - genetics N-Acetylmuramoyl-L-alanine Amidase - metabolism new subspecies Peptides Phylogenetics Phylogeny Protein Structure, Tertiary Proteins RNA, Ribosomal, 16S - genetics RNA, Ribosomal, 16S - metabolism sequence analysis signal peptide Species Specificity Staphylococcus - classification Staphylococcus - enzymology Staphylococcus aureus Staphylococcus infections trees |
| title | Phylogeny of the Staphylococcal Major Autolysin and Its Use in Genus and Species Typing |
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