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Neisseria PilC protein identified as type-4 pilus tip-located adhesin
TYPE-4 pilus-mediated adherence of Neisseria gonorrhoeae and Neisseria meningitidis is considered to be a crucial early event in neisserial infections 1,2 . In addition to the principal pilus subunit (pilin or PilE), both pathogens produce low quantities of a phase-variable PilC protein which is imp...
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| Published in: | Nature (London) 1995-01, Vol.373 (6512), p.357-359 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c464t-c878fe3cb9bbf3b948f807b8d9d865530c49fd1961587bef22222d4da4146e213 |
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| cites | cdi_FETCH-LOGICAL-c464t-c878fe3cb9bbf3b948f807b8d9d865530c49fd1961587bef22222d4da4146e213 |
| container_end_page | 359 |
| container_issue | 6512 |
| container_start_page | 357 |
| container_title | Nature (London) |
| container_volume | 373 |
| creator | Rudel, Thomas Scheuerpflug, Ina Meyer, Thomas F. |
| description | TYPE-4 pilus-mediated adherence of
Neisseria gonorrhoeae
and
Neisseria meningitidis
is considered to be a crucial early event in neisserial infections
1,2
. In addition to the principal pilus subunit (pilin or PilE), both pathogens produce low quantities of a phase-variable PilC protein which is implicated in pilus biogenesis and pilus-mediated epithelial cell adherence
3,4
. The identity, however, of the pilus adhesin has remained obscure
4,5
. Here we describe the isolation of a PilC protein from a gonococcal overproducing strain and demonstrate its specific interaction with human epithelial cells. Our results are consistent with the cell and species tropisms of neisserial infections. Binding of PilC effectively competes with pilus-mediated, but not Opa-mediated
6
, attachment of
N. gonorrhoeae
and of
N. meningitidis
, indicating that both pathogens interact with identical or very similar epithelial cell receptors. Immunogold electron microscopy using antisera raised against purified PilC and synthetic peptides locates PilC at the tip of gonococcal pili. PilC thus represents an essential pilus-associated adhesin, providing a rationale for selective protection against neisserial infections. |
| doi_str_mv | 10.1038/373357a0 |
| format | article |
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Neisseria gonorrhoeae
and
Neisseria meningitidis
is considered to be a crucial early event in neisserial infections
1,2
. In addition to the principal pilus subunit (pilin or PilE), both pathogens produce low quantities of a phase-variable PilC protein which is implicated in pilus biogenesis and pilus-mediated epithelial cell adherence
3,4
. The identity, however, of the pilus adhesin has remained obscure
4,5
. Here we describe the isolation of a PilC protein from a gonococcal overproducing strain and demonstrate its specific interaction with human epithelial cells. Our results are consistent with the cell and species tropisms of neisserial infections. Binding of PilC effectively competes with pilus-mediated, but not Opa-mediated
6
, attachment of
N. gonorrhoeae
and of
N. meningitidis
, indicating that both pathogens interact with identical or very similar epithelial cell receptors. Immunogold electron microscopy using antisera raised against purified PilC and synthetic peptides locates PilC at the tip of gonococcal pili. PilC thus represents an essential pilus-associated adhesin, providing a rationale for selective protection against neisserial infections.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/373357a0</identifier><identifier>PMID: 7830772</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adhesins, Bacterial - isolation & purification ; Adhesins, Bacterial - physiology ; Adhesins, Bacterial - ultrastructure ; Amino Acid Sequence ; Animals ; Bacteria ; Bacterial Adhesion - physiology ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - physiology ; Bacterial Proteins - ultrastructure ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Cells, Cultured ; Cellular biology ; Cloning, Molecular ; DNA, Bacterial ; Epithelium - microbiology ; Fimbriae Proteins ; Fimbriae, Bacterial - chemistry ; Fimbriae, Bacterial - physiology ; Fimbriae, Bacterial - ultrastructure ; Fundamental and applied biological sciences. Psychology ; Humanities and Social Sciences ; Humans ; letter ; Mice ; Mice, Inbred BALB C ; Microbiology ; Molecular Sequence Data ; multidisciplinary ; Neisseria gonorrhoeae ; Neisseria gonorrhoeae - physiology ; Neisseria gonorrhoeae - ultrastructure ; Neisseria meningitidis ; Neisseria meningitidis - physiology ; Neisseria meningitidis - ultrastructure ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Pathogens ; Peptides ; Protein Binding ; Proteins ; Recombinant Proteins ; Science ; Science (multidisciplinary) ; Species Specificity</subject><ispartof>Nature (London), 1995-01, Vol.373 (6512), p.357-359</ispartof><rights>Springer Nature Limited 1995</rights><rights>1995 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Jan 26, 1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c464t-c878fe3cb9bbf3b948f807b8d9d865530c49fd1961587bef22222d4da4146e213</citedby><cites>FETCH-LOGICAL-c464t-c878fe3cb9bbf3b948f807b8d9d865530c49fd1961587bef22222d4da4146e213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3422893$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7830772$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rudel, Thomas</creatorcontrib><creatorcontrib>Scheuerpflug, Ina</creatorcontrib><creatorcontrib>Meyer, Thomas F.</creatorcontrib><title>Neisseria PilC protein identified as type-4 pilus tip-located adhesin</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>TYPE-4 pilus-mediated adherence of
Neisseria gonorrhoeae
and
Neisseria meningitidis
is considered to be a crucial early event in neisserial infections
1,2
. In addition to the principal pilus subunit (pilin or PilE), both pathogens produce low quantities of a phase-variable PilC protein which is implicated in pilus biogenesis and pilus-mediated epithelial cell adherence
3,4
. The identity, however, of the pilus adhesin has remained obscure
4,5
. Here we describe the isolation of a PilC protein from a gonococcal overproducing strain and demonstrate its specific interaction with human epithelial cells. Our results are consistent with the cell and species tropisms of neisserial infections. Binding of PilC effectively competes with pilus-mediated, but not Opa-mediated
6
, attachment of
N. gonorrhoeae
and of
N. meningitidis
, indicating that both pathogens interact with identical or very similar epithelial cell receptors. Immunogold electron microscopy using antisera raised against purified PilC and synthetic peptides locates PilC at the tip of gonococcal pili. PilC thus represents an essential pilus-associated adhesin, providing a rationale for selective protection against neisserial infections.</description><subject>Adhesins, Bacterial - isolation & purification</subject><subject>Adhesins, Bacterial - physiology</subject><subject>Adhesins, Bacterial - ultrastructure</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacteria</subject><subject>Bacterial Adhesion - physiology</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - physiology</subject><subject>Bacterial Proteins - ultrastructure</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cells, Cultured</subject><subject>Cellular biology</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial</subject><subject>Epithelium - microbiology</subject><subject>Fimbriae Proteins</subject><subject>Fimbriae, Bacterial - chemistry</subject><subject>Fimbriae, Bacterial - physiology</subject><subject>Fimbriae, Bacterial - ultrastructure</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>letter</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Neisseria gonorrhoeae</subject><subject>Neisseria gonorrhoeae - physiology</subject><subject>Neisseria gonorrhoeae - ultrastructure</subject><subject>Neisseria meningitidis</subject><subject>Neisseria meningitidis - physiology</subject><subject>Neisseria meningitidis - ultrastructure</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Pathogens</subject><subject>Peptides</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Recombinant Proteins</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Species Specificity</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNqFkV9L3UAQxRdpsbcq-AUKoUhbH1J3M5PdyWO52FoQ7UP7HDb7x67kJulu8uC37168KlSw8zIM58ecYQ5jx4J_FhzoDBRArTTfYyuBSpYoSb1iK84rKjmBfMPepnTLOa-Fwn22rwi4UtWKnV-5kJKLQRc_Qr8upjjOLgxFsG6Ygw_OFjoV893kSiym0C95CFPZj0bPW83-dikMh-y1131yR7t-wH59Pf-5vigvr799X3-5LA1KnEtDirwD0zVd56FrkDxx1ZFtLMm6Bm6w8VY0UtSkOuerbVm0GgVKVwk4YB_u9-Yz_ywuze0mJOP6Xg9uXFKrlKgqUlvw48sgAkAjJWXy04ukUEpKRAT8r7uQNQmsVQbf_wPejksc8mfaiiMSUCWfjE0cU4rOt1MMGx3vWsHbbajtQ6gZfbfbt3QbZx_BXYpZP9npOhnd-6gHE9IjBpif0kDGTu-xlJXhxsWns55Z_gVLYLKK</recordid><startdate>19950126</startdate><enddate>19950126</enddate><creator>Rudel, Thomas</creator><creator>Scheuerpflug, Ina</creator><creator>Meyer, Thomas F.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>7X8</scope></search><sort><creationdate>19950126</creationdate><title>Neisseria PilC protein identified as type-4 pilus tip-located adhesin</title><author>Rudel, Thomas ; Scheuerpflug, Ina ; Meyer, Thomas F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-c878fe3cb9bbf3b948f807b8d9d865530c49fd1961587bef22222d4da4146e213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adhesins, Bacterial - isolation & purification</topic><topic>Adhesins, Bacterial - physiology</topic><topic>Adhesins, Bacterial - ultrastructure</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacteria</topic><topic>Bacterial Adhesion - physiology</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - physiology</topic><topic>Bacterial Proteins - ultrastructure</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cells, Cultured</topic><topic>Cellular biology</topic><topic>Cloning, Molecular</topic><topic>DNA, Bacterial</topic><topic>Epithelium - microbiology</topic><topic>Fimbriae Proteins</topic><topic>Fimbriae, Bacterial - chemistry</topic><topic>Fimbriae, Bacterial - physiology</topic><topic>Fimbriae, Bacterial - ultrastructure</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>letter</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>multidisciplinary</topic><topic>Neisseria gonorrhoeae</topic><topic>Neisseria gonorrhoeae - physiology</topic><topic>Neisseria gonorrhoeae - ultrastructure</topic><topic>Neisseria meningitidis</topic><topic>Neisseria meningitidis - physiology</topic><topic>Neisseria meningitidis - ultrastructure</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Pathogens</topic><topic>Peptides</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Recombinant Proteins</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rudel, Thomas</creatorcontrib><creatorcontrib>Scheuerpflug, Ina</creatorcontrib><creatorcontrib>Meyer, Thomas F.</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>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>ProQuest Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</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>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rudel, Thomas</au><au>Scheuerpflug, Ina</au><au>Meyer, Thomas F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neisseria PilC protein identified as type-4 pilus tip-located adhesin</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1995-01-26</date><risdate>1995</risdate><volume>373</volume><issue>6512</issue><spage>357</spage><epage>359</epage><pages>357-359</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>TYPE-4 pilus-mediated adherence of
Neisseria gonorrhoeae
and
Neisseria meningitidis
is considered to be a crucial early event in neisserial infections
1,2
. In addition to the principal pilus subunit (pilin or PilE), both pathogens produce low quantities of a phase-variable PilC protein which is implicated in pilus biogenesis and pilus-mediated epithelial cell adherence
3,4
. The identity, however, of the pilus adhesin has remained obscure
4,5
. Here we describe the isolation of a PilC protein from a gonococcal overproducing strain and demonstrate its specific interaction with human epithelial cells. Our results are consistent with the cell and species tropisms of neisserial infections. Binding of PilC effectively competes with pilus-mediated, but not Opa-mediated
6
, attachment of
N. gonorrhoeae
and of
N. meningitidis
, indicating that both pathogens interact with identical or very similar epithelial cell receptors. Immunogold electron microscopy using antisera raised against purified PilC and synthetic peptides locates PilC at the tip of gonococcal pili. PilC thus represents an essential pilus-associated adhesin, providing a rationale for selective protection against neisserial infections.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>7830772</pmid><doi>10.1038/373357a0</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1995-01, Vol.373 (6512), p.357-359 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77122871 |
| source | Nature Journals Online |
| subjects | Adhesins, Bacterial - isolation & purification Adhesins, Bacterial - physiology Adhesins, Bacterial - ultrastructure Amino Acid Sequence Animals Bacteria Bacterial Adhesion - physiology Bacterial Proteins - isolation & purification Bacterial Proteins - physiology Bacterial Proteins - ultrastructure Bacteriology Base Sequence Biological and medical sciences Cells, Cultured Cellular biology Cloning, Molecular DNA, Bacterial Epithelium - microbiology Fimbriae Proteins Fimbriae, Bacterial - chemistry Fimbriae, Bacterial - physiology Fimbriae, Bacterial - ultrastructure Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Humans letter Mice Mice, Inbred BALB C Microbiology Molecular Sequence Data multidisciplinary Neisseria gonorrhoeae Neisseria gonorrhoeae - physiology Neisseria gonorrhoeae - ultrastructure Neisseria meningitidis Neisseria meningitidis - physiology Neisseria meningitidis - ultrastructure Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Pathogens Peptides Protein Binding Proteins Recombinant Proteins Science Science (multidisciplinary) Species Specificity |
| title | Neisseria PilC protein identified as type-4 pilus tip-located adhesin |
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