Diversity, Distribution and Structural Prediction of the Pathogenic Bacterial Effectors EspN and EspS
Many Gram-negative enterobacteria translocate virulence proteins (effectors) into intestinal epithelial cells using a type III secretion system (T3SS) to subvert the activity of various cell functions possess. Many T3SS effectors have been extensively characterized, but there are still some effector...
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| Veröffentlicht in: | Genes 2024-09, Vol.15 (10), p.1250 |
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| creator | Li, Zhan Hu, Yuru Song, Yuan Li, Deyu Yang, Xiaolan Zhang, Liangyan Li, Tao Wang, Hui |
| description | Many Gram-negative enterobacteria translocate virulence proteins (effectors) into intestinal epithelial cells using a type III secretion system (T3SS) to subvert the activity of various cell functions possess. Many T3SS effectors have been extensively characterized, but there are still some effector proteins whose functional information is completely unknown.
In this study, two predicted effectors of unknown function, EspN and EspS (
secreted protein N and S), were selected for analysis of translocation, distribution and structure prediction.
The TEM1 (β-lactamase) translocation assay was performed, which showed that EspN and EspS are translocated into host cells in a T3SS-dependent manner during bacterial infection. A phylogenetic tree analysis revealed that homologs of EspN and EspS are widely distributed in pathogenic bacteria. Multiple sequence alignment revealed that EspN and its homologs share a conserved C-terminal region (673-1133 a.a.). Furthermore, the structure of EspN (673-1133 a.a.) was also predicted and well-defined, which showed that it has three subdomains connected by a loop region. EspS and its homologs share a sequence-conserved C-terminal (146-291 a.a.). The predicted structure of EspS (146-291 a.a.) is composed of a β-sheet consisting of four β-strands and several short helices, which has a TM score of 0.5014 with the structure of the
RTX cysteine protease domain (PDBID: 3eeb).
These results suggest that EspN and EspS may represent two important classes of T3SS effectors associated with pathogen virulence, and our findings provide important clues to understanding the potential functions of EspN and EspS. |
| doi_str_mv | 10.3390/genes15101250 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11507257</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A814119234</galeid><sourcerecordid>A814119234</sourcerecordid><originalsourceid>FETCH-LOGICAL-c369t-3a6e7314e062197a1cabc81d3a0458091d27aa41f04d3c8202acf3a137fc681a3</originalsourceid><addsrcrecordid>eNptkstPGzEQh62qqKCUY6_VSr300KUeP_ZxqnikDwlRJNqz5XjHidHGTm0vEv99HaCUIOyDR55vfvPQEPIO6BHnPf28RI8JJFBgkr4iB4y2vBaCyddP7H1ymNI1LUdQRql8Q_Z5L2TLW3FA8MzdYEwu336qzlzK0S2m7IKvtB-qqxwnk6eox-oy4uDMnSfYKq-wutR5FUoBzlQn2mSMrmBza9HkEFM1T5uLO5FiXL0le1aPCQ8f3hn5_XX-6_R7ff7z24_T4_Pa8KbPNdcNthwE0oZB32owemE6GLimQna0h4G1WguwVAzcdIwybSzXwFtrmg40n5Ev97qbabHGwaDPpXi1iW6t460K2qldj3crtQw3CkDSlpWZzMjHB4UY_kyYslq7ZHActccwJcWBQalOCFHQD8_Q6zBFX_rbUrSRTUPlf2qpR1TO21ASm62oOu5AAPSMb7WOXqDKHXDtTPBoXfnfCajvA0wMKUW0j00CVdvdUDu7Ufj3TyfzSP_bBP4XNlezpQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3120656605</pqid></control><display><type>article</type><title>Diversity, Distribution and Structural Prediction of the Pathogenic Bacterial Effectors EspN and EspS</title><source>MDPI - Multidisciplinary Digital Publishing Institute</source><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>PubMed Central Open Access</source><creator>Li, Zhan ; Hu, Yuru ; Song, Yuan ; Li, Deyu ; Yang, Xiaolan ; Zhang, Liangyan ; Li, Tao ; Wang, Hui</creator><creatorcontrib>Li, Zhan ; Hu, Yuru ; Song, Yuan ; Li, Deyu ; Yang, Xiaolan ; Zhang, Liangyan ; Li, Tao ; Wang, Hui</creatorcontrib><description>Many Gram-negative enterobacteria translocate virulence proteins (effectors) into intestinal epithelial cells using a type III secretion system (T3SS) to subvert the activity of various cell functions possess. Many T3SS effectors have been extensively characterized, but there are still some effector proteins whose functional information is completely unknown.
In this study, two predicted effectors of unknown function, EspN and EspS (
secreted protein N and S), were selected for analysis of translocation, distribution and structure prediction.
The TEM1 (β-lactamase) translocation assay was performed, which showed that EspN and EspS are translocated into host cells in a T3SS-dependent manner during bacterial infection. A phylogenetic tree analysis revealed that homologs of EspN and EspS are widely distributed in pathogenic bacteria. Multiple sequence alignment revealed that EspN and its homologs share a conserved C-terminal region (673-1133 a.a.). Furthermore, the structure of EspN (673-1133 a.a.) was also predicted and well-defined, which showed that it has three subdomains connected by a loop region. EspS and its homologs share a sequence-conserved C-terminal (146-291 a.a.). The predicted structure of EspS (146-291 a.a.) is composed of a β-sheet consisting of four β-strands and several short helices, which has a TM score of 0.5014 with the structure of the
RTX cysteine protease domain (PDBID: 3eeb).
These results suggest that EspN and EspS may represent two important classes of T3SS effectors associated with pathogen virulence, and our findings provide important clues to understanding the potential functions of EspN and EspS.</description><identifier>ISSN: 2073-4425</identifier><identifier>EISSN: 2073-4425</identifier><identifier>DOI: 10.3390/genes15101250</identifier><identifier>PMID: 39457374</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acids ; beta-Lactamases - chemistry ; beta-Lactamases - genetics ; beta-Lactamases - metabolism ; Cable television broadcasting industry ; Conserved sequence ; Cysteine ; Cysteine proteinase ; E coli ; Epithelial cells ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli - pathogenicity ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Health aspects ; Humans ; Infection ; Infections ; Inflammatory bowel disease ; International economic relations ; Nucleotide sequence ; Pathogens ; Phylogenetics ; Phylogeny ; Proteases ; Protein structure ; Protein transport ; Proteins ; Salmonella ; Type III Secretion Systems - genetics ; Type III Secretion Systems - metabolism ; Virulence ; Virulence (Microbiology) ; Virulence Factors - chemistry ; Virulence Factors - genetics ; Virulence Factors - metabolism ; β Lactamase</subject><ispartof>Genes, 2024-09, Vol.15 (10), p.1250</ispartof><rights>COPYRIGHT 2024 MDPI AG</rights><rights>2024 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2024 by the authors. 2024</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c369t-3a6e7314e062197a1cabc81d3a0458091d27aa41f04d3c8202acf3a137fc681a3</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/PMC11507257/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11507257/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39457374$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Zhan</creatorcontrib><creatorcontrib>Hu, Yuru</creatorcontrib><creatorcontrib>Song, Yuan</creatorcontrib><creatorcontrib>Li, Deyu</creatorcontrib><creatorcontrib>Yang, Xiaolan</creatorcontrib><creatorcontrib>Zhang, Liangyan</creatorcontrib><creatorcontrib>Li, Tao</creatorcontrib><creatorcontrib>Wang, Hui</creatorcontrib><title>Diversity, Distribution and Structural Prediction of the Pathogenic Bacterial Effectors EspN and EspS</title><title>Genes</title><addtitle>Genes (Basel)</addtitle><description>Many Gram-negative enterobacteria translocate virulence proteins (effectors) into intestinal epithelial cells using a type III secretion system (T3SS) to subvert the activity of various cell functions possess. Many T3SS effectors have been extensively characterized, but there are still some effector proteins whose functional information is completely unknown.
In this study, two predicted effectors of unknown function, EspN and EspS (
secreted protein N and S), were selected for analysis of translocation, distribution and structure prediction.
The TEM1 (β-lactamase) translocation assay was performed, which showed that EspN and EspS are translocated into host cells in a T3SS-dependent manner during bacterial infection. A phylogenetic tree analysis revealed that homologs of EspN and EspS are widely distributed in pathogenic bacteria. Multiple sequence alignment revealed that EspN and its homologs share a conserved C-terminal region (673-1133 a.a.). Furthermore, the structure of EspN (673-1133 a.a.) was also predicted and well-defined, which showed that it has three subdomains connected by a loop region. EspS and its homologs share a sequence-conserved C-terminal (146-291 a.a.). The predicted structure of EspS (146-291 a.a.) is composed of a β-sheet consisting of four β-strands and several short helices, which has a TM score of 0.5014 with the structure of the
RTX cysteine protease domain (PDBID: 3eeb).
These results suggest that EspN and EspS may represent two important classes of T3SS effectors associated with pathogen virulence, and our findings provide important clues to understanding the potential functions of EspN and EspS.</description><subject>Amino acids</subject><subject>beta-Lactamases - chemistry</subject><subject>beta-Lactamases - genetics</subject><subject>beta-Lactamases - metabolism</subject><subject>Cable television broadcasting industry</subject><subject>Conserved sequence</subject><subject>Cysteine</subject><subject>Cysteine proteinase</subject><subject>E coli</subject><subject>Epithelial cells</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli - pathogenicity</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Infection</subject><subject>Infections</subject><subject>Inflammatory bowel disease</subject><subject>International economic relations</subject><subject>Nucleotide sequence</subject><subject>Pathogens</subject><subject>Phylogenetics</subject><subject>Phylogeny</subject><subject>Proteases</subject><subject>Protein structure</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Salmonella</subject><subject>Type III Secretion Systems - genetics</subject><subject>Type III Secretion Systems - metabolism</subject><subject>Virulence</subject><subject>Virulence (Microbiology)</subject><subject>Virulence Factors - chemistry</subject><subject>Virulence Factors - genetics</subject><subject>Virulence Factors - metabolism</subject><subject>β Lactamase</subject><issn>2073-4425</issn><issn>2073-4425</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNptkstPGzEQh62qqKCUY6_VSr300KUeP_ZxqnikDwlRJNqz5XjHidHGTm0vEv99HaCUIOyDR55vfvPQEPIO6BHnPf28RI8JJFBgkr4iB4y2vBaCyddP7H1ymNI1LUdQRql8Q_Z5L2TLW3FA8MzdYEwu336qzlzK0S2m7IKvtB-qqxwnk6eox-oy4uDMnSfYKq-wutR5FUoBzlQn2mSMrmBza9HkEFM1T5uLO5FiXL0le1aPCQ8f3hn5_XX-6_R7ff7z24_T4_Pa8KbPNdcNthwE0oZB32owemE6GLimQna0h4G1WguwVAzcdIwybSzXwFtrmg40n5Ev97qbabHGwaDPpXi1iW6t460K2qldj3crtQw3CkDSlpWZzMjHB4UY_kyYslq7ZHActccwJcWBQalOCFHQD8_Q6zBFX_rbUrSRTUPlf2qpR1TO21ASm62oOu5AAPSMb7WOXqDKHXDtTPBoXfnfCajvA0wMKUW0j00CVdvdUDu7Ufj3TyfzSP_bBP4XNlezpQ</recordid><startdate>20240926</startdate><enddate>20240926</enddate><creator>Li, Zhan</creator><creator>Hu, Yuru</creator><creator>Song, Yuan</creator><creator>Li, Deyu</creator><creator>Yang, Xiaolan</creator><creator>Zhang, Liangyan</creator><creator>Li, Tao</creator><creator>Wang, Hui</creator><general>MDPI AG</general><general>MDPI</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>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20240926</creationdate><title>Diversity, Distribution and Structural Prediction of the Pathogenic Bacterial Effectors EspN and EspS</title><author>Li, Zhan ; Hu, Yuru ; Song, Yuan ; Li, Deyu ; Yang, Xiaolan ; Zhang, Liangyan ; Li, Tao ; Wang, Hui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c369t-3a6e7314e062197a1cabc81d3a0458091d27aa41f04d3c8202acf3a137fc681a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Amino acids</topic><topic>beta-Lactamases - chemistry</topic><topic>beta-Lactamases - genetics</topic><topic>beta-Lactamases - metabolism</topic><topic>Cable television broadcasting industry</topic><topic>Conserved sequence</topic><topic>Cysteine</topic><topic>Cysteine proteinase</topic><topic>E coli</topic><topic>Epithelial cells</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli - pathogenicity</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Health aspects</topic><topic>Humans</topic><topic>Infection</topic><topic>Infections</topic><topic>Inflammatory bowel disease</topic><topic>International economic relations</topic><topic>Nucleotide sequence</topic><topic>Pathogens</topic><topic>Phylogenetics</topic><topic>Phylogeny</topic><topic>Proteases</topic><topic>Protein structure</topic><topic>Protein transport</topic><topic>Proteins</topic><topic>Salmonella</topic><topic>Type III Secretion Systems - genetics</topic><topic>Type III Secretion Systems - metabolism</topic><topic>Virulence</topic><topic>Virulence (Microbiology)</topic><topic>Virulence Factors - chemistry</topic><topic>Virulence Factors - genetics</topic><topic>Virulence Factors - metabolism</topic><topic>β Lactamase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Zhan</creatorcontrib><creatorcontrib>Hu, Yuru</creatorcontrib><creatorcontrib>Song, Yuan</creatorcontrib><creatorcontrib>Li, Deyu</creatorcontrib><creatorcontrib>Yang, Xiaolan</creatorcontrib><creatorcontrib>Zhang, Liangyan</creatorcontrib><creatorcontrib>Li, Tao</creatorcontrib><creatorcontrib>Wang, Hui</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Genes</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Zhan</au><au>Hu, Yuru</au><au>Song, Yuan</au><au>Li, Deyu</au><au>Yang, Xiaolan</au><au>Zhang, Liangyan</au><au>Li, Tao</au><au>Wang, Hui</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Diversity, Distribution and Structural Prediction of the Pathogenic Bacterial Effectors EspN and EspS</atitle><jtitle>Genes</jtitle><addtitle>Genes (Basel)</addtitle><date>2024-09-26</date><risdate>2024</risdate><volume>15</volume><issue>10</issue><spage>1250</spage><pages>1250-</pages><issn>2073-4425</issn><eissn>2073-4425</eissn><abstract>Many Gram-negative enterobacteria translocate virulence proteins (effectors) into intestinal epithelial cells using a type III secretion system (T3SS) to subvert the activity of various cell functions possess. Many T3SS effectors have been extensively characterized, but there are still some effector proteins whose functional information is completely unknown.
In this study, two predicted effectors of unknown function, EspN and EspS (
secreted protein N and S), were selected for analysis of translocation, distribution and structure prediction.
The TEM1 (β-lactamase) translocation assay was performed, which showed that EspN and EspS are translocated into host cells in a T3SS-dependent manner during bacterial infection. A phylogenetic tree analysis revealed that homologs of EspN and EspS are widely distributed in pathogenic bacteria. Multiple sequence alignment revealed that EspN and its homologs share a conserved C-terminal region (673-1133 a.a.). Furthermore, the structure of EspN (673-1133 a.a.) was also predicted and well-defined, which showed that it has three subdomains connected by a loop region. EspS and its homologs share a sequence-conserved C-terminal (146-291 a.a.). The predicted structure of EspS (146-291 a.a.) is composed of a β-sheet consisting of four β-strands and several short helices, which has a TM score of 0.5014 with the structure of the
RTX cysteine protease domain (PDBID: 3eeb).
These results suggest that EspN and EspS may represent two important classes of T3SS effectors associated with pathogen virulence, and our findings provide important clues to understanding the potential functions of EspN and EspS.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>39457374</pmid><doi>10.3390/genes15101250</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Amino acids beta-Lactamases - chemistry beta-Lactamases - genetics beta-Lactamases - metabolism Cable television broadcasting industry Conserved sequence Cysteine Cysteine proteinase E coli Epithelial cells Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli - pathogenicity Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Health aspects Humans Infection Infections Inflammatory bowel disease International economic relations Nucleotide sequence Pathogens Phylogenetics Phylogeny Proteases Protein structure Protein transport Proteins Salmonella Type III Secretion Systems - genetics Type III Secretion Systems - metabolism Virulence Virulence (Microbiology) Virulence Factors - chemistry Virulence Factors - genetics Virulence Factors - metabolism β Lactamase |
| title | Diversity, Distribution and Structural Prediction of the Pathogenic Bacterial Effectors EspN and EspS |
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