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Channel Formation by FhaC, the Outer Membrane Protein Involved in the Secretion of the Bordetella pertussis Filamentous Hemagglutinin
Many virulence factors of pathogenic microorganisms are presented at the cell surface. However, protein secretion across the outer membrane of Gram-negative bacteria remains poorly understood. Here we used the extremely efficient secretion of the Bordetella pertussis filamentous hemagglutinin (FHA)...
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| Published in: | The Journal of biological chemistry 1999-12, Vol.274 (53), p.37731-37735 |
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| container_end_page | 37735 |
| container_issue | 53 |
| container_start_page | 37731 |
| container_title | The Journal of biological chemistry |
| container_volume | 274 |
| creator | Françoise Jacob-Dubuisson Chahrazed El-Hamel Nathalie Saint Sandrine Guédin Eve Willery Gérard Molle Camille Locht |
| description | Many virulence factors of pathogenic microorganisms are presented at the cell surface. However, protein secretion across the
outer membrane of Gram-negative bacteria remains poorly understood. Here we used the extremely efficient secretion of the
Bordetella pertussis filamentous hemagglutinin (FHA) to decipher this process. FHA secretion requires a single specific accessory protein, FhaC,
the prototype of a family of proteins necessary for the extracellular localization of various virulence proteins in Gram-negative
bacteria. We show that FhaC is heat-modifiable and localized in the outer membrane. Circular dichroism spectra indicated that
FhaC is rich in β-strands, in agreement with structural predictions for this protein. We further demonstrated that FhaC forms
pores in artificial membranes, as evidenced by single-channel conductance measurements through planar lipid bilayers, as well
as by liposome swelling assays and patch-clamp experiments using proteoliposomes. Single-channel conductance appeared to fluctuate
very fast, suggesting that the FhaC channels frequently assume a closed conformation. We thus propose that FhaC forms a specific
β-barrel channel in the outer membrane for the outward translocation of FHA. |
| doi_str_mv | 10.1074/jbc.274.53.37731 |
| format | article |
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outer membrane of Gram-negative bacteria remains poorly understood. Here we used the extremely efficient secretion of the
Bordetella pertussis filamentous hemagglutinin (FHA) to decipher this process. FHA secretion requires a single specific accessory protein, FhaC,
the prototype of a family of proteins necessary for the extracellular localization of various virulence proteins in Gram-negative
bacteria. We show that FhaC is heat-modifiable and localized in the outer membrane. Circular dichroism spectra indicated that
FhaC is rich in β-strands, in agreement with structural predictions for this protein. We further demonstrated that FhaC forms
pores in artificial membranes, as evidenced by single-channel conductance measurements through planar lipid bilayers, as well
as by liposome swelling assays and patch-clamp experiments using proteoliposomes. Single-channel conductance appeared to fluctuate
very fast, suggesting that the FhaC channels frequently assume a closed conformation. We thus propose that FhaC forms a specific
β-barrel channel in the outer membrane for the outward translocation of FHA.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.53.37731</identifier><identifier>PMID: 10608832</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Bacterial Outer Membrane Proteins - isolation & purification ; Bacterial Outer Membrane Proteins - physiology ; Base Sequence ; Bordetella pertussis ; Bordetella pertussis - metabolism ; Bordetella pertussis - pathogenicity ; Chromatography, Affinity ; Chromatography, Ion Exchange ; Circular Dichroism ; DNA Primers ; FhaC protein ; Hemagglutinins - metabolism ; Hot Temperature ; Subcellular Fractions - metabolism</subject><ispartof>The Journal of biological chemistry, 1999-12, Vol.274 (53), p.37731-37735</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-504a746d87bae3b92b3e9a0d829e295223e5db23366683dc9416dda75229dd723</citedby><cites>FETCH-LOGICAL-c492t-504a746d87bae3b92b3e9a0d829e295223e5db23366683dc9416dda75229dd723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10608832$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Françoise Jacob-Dubuisson</creatorcontrib><creatorcontrib>Chahrazed El-Hamel</creatorcontrib><creatorcontrib>Nathalie Saint</creatorcontrib><creatorcontrib>Sandrine Guédin</creatorcontrib><creatorcontrib>Eve Willery</creatorcontrib><creatorcontrib>Gérard Molle</creatorcontrib><creatorcontrib>Camille Locht</creatorcontrib><title>Channel Formation by FhaC, the Outer Membrane Protein Involved in the Secretion of the Bordetella pertussis Filamentous Hemagglutinin</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Many virulence factors of pathogenic microorganisms are presented at the cell surface. However, protein secretion across the
outer membrane of Gram-negative bacteria remains poorly understood. Here we used the extremely efficient secretion of the
Bordetella pertussis filamentous hemagglutinin (FHA) to decipher this process. FHA secretion requires a single specific accessory protein, FhaC,
the prototype of a family of proteins necessary for the extracellular localization of various virulence proteins in Gram-negative
bacteria. We show that FhaC is heat-modifiable and localized in the outer membrane. Circular dichroism spectra indicated that
FhaC is rich in β-strands, in agreement with structural predictions for this protein. We further demonstrated that FhaC forms
pores in artificial membranes, as evidenced by single-channel conductance measurements through planar lipid bilayers, as well
as by liposome swelling assays and patch-clamp experiments using proteoliposomes. Single-channel conductance appeared to fluctuate
very fast, suggesting that the FhaC channels frequently assume a closed conformation. We thus propose that FhaC forms a specific
β-barrel channel in the outer membrane for the outward translocation of FHA.</description><subject>Bacterial Outer Membrane Proteins - isolation & purification</subject><subject>Bacterial Outer Membrane Proteins - physiology</subject><subject>Base Sequence</subject><subject>Bordetella pertussis</subject><subject>Bordetella pertussis - metabolism</subject><subject>Bordetella pertussis - pathogenicity</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Ion Exchange</subject><subject>Circular Dichroism</subject><subject>DNA Primers</subject><subject>FhaC protein</subject><subject>Hemagglutinins - metabolism</subject><subject>Hot Temperature</subject><subject>Subcellular Fractions - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNqFkc1u1DAURi0EokPLnhXyArEig3_iOF7CqNNWKioSRWJn2fGdiavEHmynVR-A9yYz00VZ4Y2t6_N9utJB6B0lS0pk_fnOdksm66XgSy4lpy_QgpKWV1zQXy_RghBGK8VEe4Le5HxH5lMr-hqdUNKQtuVsgf6sehMCDHgd02iKjwHbR7zuzeoTLj3gm6lAwt9gtMkEwN9TLOADvgr3cbgHh-f3HvsBXYJDOm4Og68xOSgwDAbvIJUpZ5_x2g9mhFDilPEljGa7Habigw9n6NXGDBnePt2n6Of6_HZ1WV3fXFytvlxXXa1YqQSpjawb10prgFvFLAdliGuZAqYEYxyEs4zzpmla7jpV08Y5I-cf5Zxk_BR9PPbuUvw9QS569LnbbxlgXko3irdESPFfkMpaNJztQXIEuxRzTrDRu-RHkx41JXrvSM-O9OxIC64PjubI-6fuyY7gngWOUmbgwxHo_bZ_8Am09bHrYfy35y_q6JoK</recordid><startdate>19991231</startdate><enddate>19991231</enddate><creator>Françoise Jacob-Dubuisson</creator><creator>Chahrazed El-Hamel</creator><creator>Nathalie Saint</creator><creator>Sandrine Guédin</creator><creator>Eve Willery</creator><creator>Gérard Molle</creator><creator>Camille Locht</creator><general>American Society for Biochemistry and Molecular Biology</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>C1K</scope><scope>7X8</scope></search><sort><creationdate>19991231</creationdate><title>Channel Formation by FhaC, the Outer Membrane Protein Involved in the Secretion of the Bordetella pertussis Filamentous Hemagglutinin</title><author>Françoise Jacob-Dubuisson ; Chahrazed El-Hamel ; Nathalie Saint ; Sandrine Guédin ; Eve Willery ; Gérard Molle ; Camille Locht</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-504a746d87bae3b92b3e9a0d829e295223e5db23366683dc9416dda75229dd723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Bacterial Outer Membrane Proteins - isolation & purification</topic><topic>Bacterial Outer Membrane Proteins - physiology</topic><topic>Base Sequence</topic><topic>Bordetella pertussis</topic><topic>Bordetella pertussis - metabolism</topic><topic>Bordetella pertussis - pathogenicity</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Ion Exchange</topic><topic>Circular Dichroism</topic><topic>DNA Primers</topic><topic>FhaC protein</topic><topic>Hemagglutinins - metabolism</topic><topic>Hot Temperature</topic><topic>Subcellular Fractions - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Françoise Jacob-Dubuisson</creatorcontrib><creatorcontrib>Chahrazed El-Hamel</creatorcontrib><creatorcontrib>Nathalie Saint</creatorcontrib><creatorcontrib>Sandrine Guédin</creatorcontrib><creatorcontrib>Eve Willery</creatorcontrib><creatorcontrib>Gérard Molle</creatorcontrib><creatorcontrib>Camille Locht</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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Françoise Jacob-Dubuisson</au><au>Chahrazed El-Hamel</au><au>Nathalie Saint</au><au>Sandrine Guédin</au><au>Eve Willery</au><au>Gérard Molle</au><au>Camille Locht</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Channel Formation by FhaC, the Outer Membrane Protein Involved in the Secretion of the Bordetella pertussis Filamentous Hemagglutinin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-12-31</date><risdate>1999</risdate><volume>274</volume><issue>53</issue><spage>37731</spage><epage>37735</epage><pages>37731-37735</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Many virulence factors of pathogenic microorganisms are presented at the cell surface. However, protein secretion across the
outer membrane of Gram-negative bacteria remains poorly understood. Here we used the extremely efficient secretion of the
Bordetella pertussis filamentous hemagglutinin (FHA) to decipher this process. FHA secretion requires a single specific accessory protein, FhaC,
the prototype of a family of proteins necessary for the extracellular localization of various virulence proteins in Gram-negative
bacteria. We show that FhaC is heat-modifiable and localized in the outer membrane. Circular dichroism spectra indicated that
FhaC is rich in β-strands, in agreement with structural predictions for this protein. We further demonstrated that FhaC forms
pores in artificial membranes, as evidenced by single-channel conductance measurements through planar lipid bilayers, as well
as by liposome swelling assays and patch-clamp experiments using proteoliposomes. Single-channel conductance appeared to fluctuate
very fast, suggesting that the FhaC channels frequently assume a closed conformation. We thus propose that FhaC forms a specific
β-barrel channel in the outer membrane for the outward translocation of FHA.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>10608832</pmid><doi>10.1074/jbc.274.53.37731</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1999-12, Vol.274 (53), p.37731-37735 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69380575 |
| source | ScienceDirect (Online service) |
| subjects | Bacterial Outer Membrane Proteins - isolation & purification Bacterial Outer Membrane Proteins - physiology Base Sequence Bordetella pertussis Bordetella pertussis - metabolism Bordetella pertussis - pathogenicity Chromatography, Affinity Chromatography, Ion Exchange Circular Dichroism DNA Primers FhaC protein Hemagglutinins - metabolism Hot Temperature Subcellular Fractions - metabolism |
| title | Channel Formation by FhaC, the Outer Membrane Protein Involved in the Secretion of the Bordetella pertussis Filamentous Hemagglutinin |
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