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Crucial domains are conserved in Enterobacteriaceae porins
Abstract With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram-negative bacterial porins using anti-pep...
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| Published in: | FEMS microbiology letters 1996-02, Vol.136 (1), p.91-97 |
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| Main Authors: | , , , , |
| Format: | Article |
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| cites | cdi_FETCH-LOGICAL-c4861-638fa6fde0bfff360b237be3eb92e3b1f435a94eb44ad7c074eb1f2f30d348843 |
| container_end_page | 97 |
| container_issue | 1 |
| container_start_page | 91 |
| container_title | FEMS microbiology letters |
| container_volume | 136 |
| creator | Simonet, Valérie Malléa, Monique Fourel, Didier Bolla, Jean-Michel Pages, Jean-Marie |
| description | Abstract
With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram-negative bacterial porins using anti-peptide antibodies specific to exposed, transmembrane spanning, or pore-forming regions of Escherichia coli porins. Anti-peptide antibodies which recognized the exposed epitopes indicated a great variability among the bacterial porins analysed. Interestingly, an antigenic site located in the internal loop L3 constricting the pore diameter was present in the majority of the bacterial porins tested. Two epitopes located in domains involved in subunit interaction were also highly conserved. The presence of these common peptides suggested a conservation of specific regions involved in the functional organization of the enterobacterial porins. |
| doi_str_mv | 10.1111/j.1574-6968.1996.tb08030.x |
| format | article |
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With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram-negative bacterial porins using anti-peptide antibodies specific to exposed, transmembrane spanning, or pore-forming regions of Escherichia coli porins. Anti-peptide antibodies which recognized the exposed epitopes indicated a great variability among the bacterial porins analysed. Interestingly, an antigenic site located in the internal loop L3 constricting the pore diameter was present in the majority of the bacterial porins tested. Two epitopes located in domains involved in subunit interaction were also highly conserved. The presence of these common peptides suggested a conservation of specific regions involved in the functional organization of the enterobacterial porins.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1996.tb08030.x</identifier><identifier>PMID: 8919461</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Antibiotic resistance ; Antibodies ; Antigens ; Antigens, Bacterial - chemistry ; Antigens, Bacterial - genetics ; Anti‐peptide antibodies ; Bacteria ; Bacterial porins ; Bacteriology ; Biological and medical sciences ; Conserved Sequence ; Cross Reactions ; Crystal structure ; Domains ; E coli ; Enterobacteriaceae ; Enterobacteriaceae - genetics ; Enterobacteriaceae - immunology ; Epitopes ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - immunology ; Functional morphology ; Fundamental and applied biological sciences. Psychology ; Gram-negative bacteria ; Gram-Negative Bacteria - genetics ; Gram-Negative Bacteria - immunology ; Immunochemistry ; Microbiology ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Peptides ; Permeability, membrane transport, intracellular transport ; Plasmids ; Pore formation ; Porins ; Porins - chemistry ; Porins - genetics ; Porins - immunology</subject><ispartof>FEMS microbiology letters, 1996-02, Vol.136 (1), p.91-97</ispartof><rights>1996 Federation of European Microbiological Societies. All rights reserved 1996</rights><rights>1996 INIST-CNRS</rights><rights>1996 Federation of European Microbiological Societies. All rights reserved</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4861-638fa6fde0bfff360b237be3eb92e3b1f435a94eb44ad7c074eb1f2f30d348843</citedby><cites>FETCH-LOGICAL-c4861-638fa6fde0bfff360b237be3eb92e3b1f435a94eb44ad7c074eb1f2f30d348843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3011001$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8919461$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Simonet, Valérie</creatorcontrib><creatorcontrib>Malléa, Monique</creatorcontrib><creatorcontrib>Fourel, Didier</creatorcontrib><creatorcontrib>Bolla, Jean-Michel</creatorcontrib><creatorcontrib>Pages, Jean-Marie</creatorcontrib><title>Crucial domains are conserved in Enterobacteriaceae porins</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram-negative bacterial porins using anti-peptide antibodies specific to exposed, transmembrane spanning, or pore-forming regions of Escherichia coli porins. Anti-peptide antibodies which recognized the exposed epitopes indicated a great variability among the bacterial porins analysed. Interestingly, an antigenic site located in the internal loop L3 constricting the pore diameter was present in the majority of the bacterial porins tested. Two epitopes located in domains involved in subunit interaction were also highly conserved. The presence of these common peptides suggested a conservation of specific regions involved in the functional organization of the enterobacterial porins.</description><subject>Amino Acid Sequence</subject><subject>Antibiotic resistance</subject><subject>Antibodies</subject><subject>Antigens</subject><subject>Antigens, Bacterial - chemistry</subject><subject>Antigens, Bacterial - genetics</subject><subject>Anti‐peptide antibodies</subject><subject>Bacteria</subject><subject>Bacterial porins</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Conserved Sequence</subject><subject>Cross Reactions</subject><subject>Crystal structure</subject><subject>Domains</subject><subject>E coli</subject><subject>Enterobacteriaceae</subject><subject>Enterobacteriaceae - genetics</subject><subject>Enterobacteriaceae - immunology</subject><subject>Epitopes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - immunology</subject><subject>Functional morphology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gram-negative bacteria</subject><subject>Gram-Negative Bacteria - genetics</subject><subject>Gram-Negative Bacteria - immunology</subject><subject>Immunochemistry</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Mutagenesis, Site-Directed</subject><subject>Peptides</subject><subject>Permeability, membrane transport, intracellular transport</subject><subject>Plasmids</subject><subject>Pore formation</subject><subject>Porins</subject><subject>Porins - chemistry</subject><subject>Porins - genetics</subject><subject>Porins - immunology</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqVkMFq3DAURUVpSadpP6Fg0tCd3SdLlqVAF2VI0sKUbNK1kOQn8OCxptK4Tf4-MmNmUZJFtXmCd650OYRcUKhoPl-2FW1aXgolZEWVEtXBggQG1cMrsjqtXpMVsFaWFFT7lrxLaQsAvAZxRs6koooLuiJX6zi53gxFF3amH1NhIhYujAnjH-yKfiyuxwPGYI3LozcODRb7EDP6nrzxZkj4YZnn5NfN9f36e7m5u_2x_rYpHZeCloJJb4TvEKz3ngmwNWstMrSqRmap56wxiqPl3HStgzZfqa89g45xKTk7J5-P7-5j-D1hOuhdnxwOgxkxTElTwTlXTZPBT_-A2zDFMXfTNWNUgsh9MnV1pFwMKUX0eh_7nYmPmoKe9eqtnh3q2aGe9epFr37I4Y_LF5PdYXeKLj7z_nLZm-TM4KMZXZ9OGANKAWbs6xH72w_4-B8F9M3PjZrzzTEfpv0L6fK5-k8H5aYa</recordid><startdate>199602</startdate><enddate>199602</enddate><creator>Simonet, Valérie</creator><creator>Malléa, Monique</creator><creator>Fourel, Didier</creator><creator>Bolla, Jean-Michel</creator><creator>Pages, Jean-Marie</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>199602</creationdate><title>Crucial domains are conserved in Enterobacteriaceae porins</title><author>Simonet, Valérie ; Malléa, Monique ; Fourel, Didier ; Bolla, Jean-Michel ; Pages, Jean-Marie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4861-638fa6fde0bfff360b237be3eb92e3b1f435a94eb44ad7c074eb1f2f30d348843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>Antibiotic resistance</topic><topic>Antibodies</topic><topic>Antigens</topic><topic>Antigens, Bacterial - chemistry</topic><topic>Antigens, Bacterial - genetics</topic><topic>Anti‐peptide antibodies</topic><topic>Bacteria</topic><topic>Bacterial porins</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Conserved Sequence</topic><topic>Cross Reactions</topic><topic>Crystal structure</topic><topic>Domains</topic><topic>E coli</topic><topic>Enterobacteriaceae</topic><topic>Enterobacteriaceae - genetics</topic><topic>Enterobacteriaceae - immunology</topic><topic>Epitopes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - immunology</topic><topic>Functional morphology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gram-negative bacteria</topic><topic>Gram-Negative Bacteria - genetics</topic><topic>Gram-Negative Bacteria - immunology</topic><topic>Immunochemistry</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Mutagenesis, Site-Directed</topic><topic>Peptides</topic><topic>Permeability, membrane transport, intracellular transport</topic><topic>Plasmids</topic><topic>Pore formation</topic><topic>Porins</topic><topic>Porins - chemistry</topic><topic>Porins - genetics</topic><topic>Porins - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Simonet, Valérie</creatorcontrib><creatorcontrib>Malléa, Monique</creatorcontrib><creatorcontrib>Fourel, Didier</creatorcontrib><creatorcontrib>Bolla, Jean-Michel</creatorcontrib><creatorcontrib>Pages, Jean-Marie</creatorcontrib><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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Simonet, Valérie</au><au>Malléa, Monique</au><au>Fourel, Didier</au><au>Bolla, Jean-Michel</au><au>Pages, Jean-Marie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crucial domains are conserved in Enterobacteriaceae porins</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>1996-02</date><risdate>1996</risdate><volume>136</volume><issue>1</issue><spage>91</spage><epage>97</epage><pages>91-97</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram-negative bacterial porins using anti-peptide antibodies specific to exposed, transmembrane spanning, or pore-forming regions of Escherichia coli porins. Anti-peptide antibodies which recognized the exposed epitopes indicated a great variability among the bacterial porins analysed. Interestingly, an antigenic site located in the internal loop L3 constricting the pore diameter was present in the majority of the bacterial porins tested. Two epitopes located in domains involved in subunit interaction were also highly conserved. The presence of these common peptides suggested a conservation of specific regions involved in the functional organization of the enterobacterial porins.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8919461</pmid><doi>10.1111/j.1574-6968.1996.tb08030.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 1996-02, Vol.136 (1), p.91-97 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16444955 |
| source | Oxford Journals Online |
| subjects | Amino Acid Sequence Antibiotic resistance Antibodies Antigens Antigens, Bacterial - chemistry Antigens, Bacterial - genetics Anti‐peptide antibodies Bacteria Bacterial porins Bacteriology Biological and medical sciences Conserved Sequence Cross Reactions Crystal structure Domains E coli Enterobacteriaceae Enterobacteriaceae - genetics Enterobacteriaceae - immunology Epitopes Escherichia coli Escherichia coli - genetics Escherichia coli - immunology Functional morphology Fundamental and applied biological sciences. Psychology Gram-negative bacteria Gram-Negative Bacteria - genetics Gram-Negative Bacteria - immunology Immunochemistry Microbiology Molecular Sequence Data Molecular Structure Mutagenesis, Site-Directed Peptides Permeability, membrane transport, intracellular transport Plasmids Pore formation Porins Porins - chemistry Porins - genetics Porins - immunology |
| title | Crucial domains are conserved in Enterobacteriaceae porins |
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