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The contrasting mechanisms of serum resistance of Neisseria gonorrhoeae and group B Neisseria meningitidis
Neisseria gonorrhoeae and Neisseria meningitidis have evolved intricate mechanisms to evade complement-mediated killing. Sialylation of gonococcal lipooligosaccharide (LOS) results in conversion of previously serum sensitive strains to unstable serum resistance, which is mediated by factor H binding...
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| Published in: | Molecular immunology 1999-09, Vol.36 (13), p.915-928 |
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| Main Authors: | , , , , , , , , , , , |
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| container_end_page | 928 |
| container_issue | 13 |
| container_start_page | 915 |
| container_title | Molecular immunology |
| container_volume | 36 |
| creator | Ram, S Mackinnon, F.G Gulati, S McQuillen, D.P Vogel, U Frosch, M Elkins, C Guttormsen, H.-K Wetzler, L.M Oppermann, M Pangburn, M.K Rice, P.A |
| description | Neisseria gonorrhoeae and
Neisseria meningitidis have evolved intricate mechanisms to evade complement-mediated killing. Sialylation of gonococcal lipooligosaccharide (LOS) results in conversion of previously serum sensitive strains to unstable serum resistance, which is mediated by factor H binding. Porin (Por) is also instrumental in mediating stable serum resistance in gonococci. The 5th loop of certain gonococcal Por1As binds factor H, which efficiently inactivates C3b to iC3b. Factor H glycan residues may be essential for factor H binding to certain Por1A strains. Por1A strains can also regulate the classical pathway by binding to C4b-binding protein (C4bp) probably via the 1st loop of the Por molecule. Certain serum resistant Por1B strains can also regulate complement by binding C4bp through a loop other than loop 1. Purified C4b can inhibit binding of C4bp to Por 1B, but not Por1A, suggesting different binding sites on C4bp for the two Por types. Unlike serum resistant gonococci, resistant meningococci have abundant C3b on their surface, which is only partially processed to iC3b. The main mechanism of complement evasion by group B meningococci is inhibition of membrane attack complex (MAC) insertion by their polysaccharide capsule. LOS structure may act in concert with capsule to prevent MAC insertion. Meningococcal strains with Class 3 Por preferentially bind factor H, suggesting Class 3 Por acts as a receptor for factor H. |
| doi_str_mv | 10.1016/S0161-5890(99)00114-5 |
| format | article |
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Neisseria meningitidis have evolved intricate mechanisms to evade complement-mediated killing. Sialylation of gonococcal lipooligosaccharide (LOS) results in conversion of previously serum sensitive strains to unstable serum resistance, which is mediated by factor H binding. Porin (Por) is also instrumental in mediating stable serum resistance in gonococci. The 5th loop of certain gonococcal Por1As binds factor H, which efficiently inactivates C3b to iC3b. Factor H glycan residues may be essential for factor H binding to certain Por1A strains. Por1A strains can also regulate the classical pathway by binding to C4b-binding protein (C4bp) probably via the 1st loop of the Por molecule. Certain serum resistant Por1B strains can also regulate complement by binding C4bp through a loop other than loop 1. Purified C4b can inhibit binding of C4bp to Por 1B, but not Por1A, suggesting different binding sites on C4bp for the two Por types. Unlike serum resistant gonococci, resistant meningococci have abundant C3b on their surface, which is only partially processed to iC3b. The main mechanism of complement evasion by group B meningococci is inhibition of membrane attack complex (MAC) insertion by their polysaccharide capsule. LOS structure may act in concert with capsule to prevent MAC insertion. Meningococcal strains with Class 3 Por preferentially bind factor H, suggesting Class 3 Por acts as a receptor for factor H.</description><identifier>ISSN: 0161-5890</identifier><identifier>EISSN: 1872-9142</identifier><identifier>DOI: 10.1016/S0161-5890(99)00114-5</identifier><identifier>PMID: 10698346</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Blood Bactericidal Activity - immunology ; C4b-binding protein ; Capsular polysaccharide ; Complement ; complement component C4b-binding protein ; complement factor H ; Complement System Proteins - metabolism ; Factor H ; Humans ; In Vitro Techniques ; lipooligosaccharides ; Lipopolysaccharides - chemistry ; Lipopolysaccharides - immunology ; Neisseria gonorrhoeae ; Neisseria gonorrhoeae - immunology ; Neisseria gonorrhoeae - pathogenicity ; Neisseria meningitidis ; Neisseria meningitidis - classification ; Neisseria meningitidis - immunology ; Neisseria meningitidis - pathogenicity ; Por1A protein ; Porin ; Porins - immunology ; Species Specificity</subject><ispartof>Molecular immunology, 1999-09, Vol.36 (13), p.915-928</ispartof><rights>1999 Elsevier Science Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-31d7002e0e7202f9e882ef3b041701dfd3a546405368c550cb89a854d50692bf3</citedby><cites>FETCH-LOGICAL-c441t-31d7002e0e7202f9e882ef3b041701dfd3a546405368c550cb89a854d50692bf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10698346$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ram, S</creatorcontrib><creatorcontrib>Mackinnon, F.G</creatorcontrib><creatorcontrib>Gulati, S</creatorcontrib><creatorcontrib>McQuillen, D.P</creatorcontrib><creatorcontrib>Vogel, U</creatorcontrib><creatorcontrib>Frosch, M</creatorcontrib><creatorcontrib>Elkins, C</creatorcontrib><creatorcontrib>Guttormsen, H.-K</creatorcontrib><creatorcontrib>Wetzler, L.M</creatorcontrib><creatorcontrib>Oppermann, M</creatorcontrib><creatorcontrib>Pangburn, M.K</creatorcontrib><creatorcontrib>Rice, P.A</creatorcontrib><title>The contrasting mechanisms of serum resistance of Neisseria gonorrhoeae and group B Neisseria meningitidis</title><title>Molecular immunology</title><addtitle>Mol Immunol</addtitle><description>Neisseria gonorrhoeae and
Neisseria meningitidis have evolved intricate mechanisms to evade complement-mediated killing. Sialylation of gonococcal lipooligosaccharide (LOS) results in conversion of previously serum sensitive strains to unstable serum resistance, which is mediated by factor H binding. Porin (Por) is also instrumental in mediating stable serum resistance in gonococci. The 5th loop of certain gonococcal Por1As binds factor H, which efficiently inactivates C3b to iC3b. Factor H glycan residues may be essential for factor H binding to certain Por1A strains. Por1A strains can also regulate the classical pathway by binding to C4b-binding protein (C4bp) probably via the 1st loop of the Por molecule. Certain serum resistant Por1B strains can also regulate complement by binding C4bp through a loop other than loop 1. Purified C4b can inhibit binding of C4bp to Por 1B, but not Por1A, suggesting different binding sites on C4bp for the two Por types. Unlike serum resistant gonococci, resistant meningococci have abundant C3b on their surface, which is only partially processed to iC3b. The main mechanism of complement evasion by group B meningococci is inhibition of membrane attack complex (MAC) insertion by their polysaccharide capsule. LOS structure may act in concert with capsule to prevent MAC insertion. Meningococcal strains with Class 3 Por preferentially bind factor H, suggesting Class 3 Por acts as a receptor for factor H.</description><subject>Blood Bactericidal Activity - immunology</subject><subject>C4b-binding protein</subject><subject>Capsular polysaccharide</subject><subject>Complement</subject><subject>complement component C4b-binding protein</subject><subject>complement factor H</subject><subject>Complement System Proteins - metabolism</subject><subject>Factor H</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>lipooligosaccharides</subject><subject>Lipopolysaccharides - chemistry</subject><subject>Lipopolysaccharides - immunology</subject><subject>Neisseria gonorrhoeae</subject><subject>Neisseria gonorrhoeae - immunology</subject><subject>Neisseria gonorrhoeae - pathogenicity</subject><subject>Neisseria meningitidis</subject><subject>Neisseria meningitidis - classification</subject><subject>Neisseria meningitidis - immunology</subject><subject>Neisseria meningitidis - pathogenicity</subject><subject>Por1A protein</subject><subject>Porin</subject><subject>Porins - immunology</subject><subject>Species Specificity</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNqFkUFP3DAQha2qqGxpf0Irnyp6CB0ndmKfECBokRA9lJ4trz3ZNdrEiyep1H-Pl0WIG5cZafS9Gc17jH0RcCJAtD_-lCIqpQ0cG_MdQAhZqXdsIXRXV0bI-j1bvCCH7CPRPQC00KoP7FBAa3Qj2wW7v1sj92mcsqMpjis-oF-7MdJAPPWcMM8Dz0iRJjd63M1uMVKZR8dXaUw5rxM65G4MfJXTvOXnr4gBx7I0TjFE-sQOerch_Pzcj9jfq8u7i1_Vze-f1xdnN5WXUkxVI0IHUCNgV0PdG9S6xr5ZghQdiNCHxinZSlBNq71S4JfaOK1kUOWpetk3R-zbfu82p4cZabJDJI-bjRsxzWRbI6WsBbwJik5pbVRXQLUHfU5EGXu7zXFw-b8VYHdp2Kc07M5qa4x9SsOqovv6fGBeDhheqfb2F-B0D2Dx41_EbMlHLD6HmNFPNqT4xolHM3SaCg</recordid><startdate>19990901</startdate><enddate>19990901</enddate><creator>Ram, S</creator><creator>Mackinnon, F.G</creator><creator>Gulati, S</creator><creator>McQuillen, D.P</creator><creator>Vogel, U</creator><creator>Frosch, M</creator><creator>Elkins, C</creator><creator>Guttormsen, H.-K</creator><creator>Wetzler, L.M</creator><creator>Oppermann, M</creator><creator>Pangburn, M.K</creator><creator>Rice, P.A</creator><general>Elsevier Ltd</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>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19990901</creationdate><title>The contrasting mechanisms of serum resistance of Neisseria gonorrhoeae and group B Neisseria meningitidis</title><author>Ram, S ; Mackinnon, F.G ; Gulati, S ; McQuillen, D.P ; Vogel, U ; Frosch, M ; Elkins, C ; Guttormsen, H.-K ; Wetzler, L.M ; Oppermann, M ; Pangburn, M.K ; Rice, P.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441t-31d7002e0e7202f9e882ef3b041701dfd3a546405368c550cb89a854d50692bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Blood Bactericidal Activity - immunology</topic><topic>C4b-binding protein</topic><topic>Capsular polysaccharide</topic><topic>Complement</topic><topic>complement component C4b-binding protein</topic><topic>complement factor H</topic><topic>Complement System Proteins - metabolism</topic><topic>Factor H</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>lipooligosaccharides</topic><topic>Lipopolysaccharides - chemistry</topic><topic>Lipopolysaccharides - immunology</topic><topic>Neisseria gonorrhoeae</topic><topic>Neisseria gonorrhoeae - immunology</topic><topic>Neisseria gonorrhoeae - pathogenicity</topic><topic>Neisseria meningitidis</topic><topic>Neisseria meningitidis - classification</topic><topic>Neisseria meningitidis - immunology</topic><topic>Neisseria meningitidis - pathogenicity</topic><topic>Por1A protein</topic><topic>Porin</topic><topic>Porins - immunology</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ram, S</creatorcontrib><creatorcontrib>Mackinnon, F.G</creatorcontrib><creatorcontrib>Gulati, S</creatorcontrib><creatorcontrib>McQuillen, D.P</creatorcontrib><creatorcontrib>Vogel, U</creatorcontrib><creatorcontrib>Frosch, M</creatorcontrib><creatorcontrib>Elkins, C</creatorcontrib><creatorcontrib>Guttormsen, H.-K</creatorcontrib><creatorcontrib>Wetzler, L.M</creatorcontrib><creatorcontrib>Oppermann, M</creatorcontrib><creatorcontrib>Pangburn, M.K</creatorcontrib><creatorcontrib>Rice, P.A</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>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ram, S</au><au>Mackinnon, F.G</au><au>Gulati, S</au><au>McQuillen, D.P</au><au>Vogel, U</au><au>Frosch, M</au><au>Elkins, C</au><au>Guttormsen, H.-K</au><au>Wetzler, L.M</au><au>Oppermann, M</au><au>Pangburn, M.K</au><au>Rice, P.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The contrasting mechanisms of serum resistance of Neisseria gonorrhoeae and group B Neisseria meningitidis</atitle><jtitle>Molecular immunology</jtitle><addtitle>Mol Immunol</addtitle><date>1999-09-01</date><risdate>1999</risdate><volume>36</volume><issue>13</issue><spage>915</spage><epage>928</epage><pages>915-928</pages><issn>0161-5890</issn><eissn>1872-9142</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><notes>ObjectType-Feature-3</notes><notes>ObjectType-Review-1</notes><abstract>Neisseria gonorrhoeae and
Neisseria meningitidis have evolved intricate mechanisms to evade complement-mediated killing. Sialylation of gonococcal lipooligosaccharide (LOS) results in conversion of previously serum sensitive strains to unstable serum resistance, which is mediated by factor H binding. Porin (Por) is also instrumental in mediating stable serum resistance in gonococci. The 5th loop of certain gonococcal Por1As binds factor H, which efficiently inactivates C3b to iC3b. Factor H glycan residues may be essential for factor H binding to certain Por1A strains. Por1A strains can also regulate the classical pathway by binding to C4b-binding protein (C4bp) probably via the 1st loop of the Por molecule. Certain serum resistant Por1B strains can also regulate complement by binding C4bp through a loop other than loop 1. Purified C4b can inhibit binding of C4bp to Por 1B, but not Por1A, suggesting different binding sites on C4bp for the two Por types. Unlike serum resistant gonococci, resistant meningococci have abundant C3b on their surface, which is only partially processed to iC3b. The main mechanism of complement evasion by group B meningococci is inhibition of membrane attack complex (MAC) insertion by their polysaccharide capsule. LOS structure may act in concert with capsule to prevent MAC insertion. Meningococcal strains with Class 3 Por preferentially bind factor H, suggesting Class 3 Por acts as a receptor for factor H.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>10698346</pmid><doi>10.1016/S0161-5890(99)00114-5</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular immunology, 1999-09, Vol.36 (13), p.915-928 |
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| source | Elsevier |
| subjects | Blood Bactericidal Activity - immunology C4b-binding protein Capsular polysaccharide Complement complement component C4b-binding protein complement factor H Complement System Proteins - metabolism Factor H Humans In Vitro Techniques lipooligosaccharides Lipopolysaccharides - chemistry Lipopolysaccharides - immunology Neisseria gonorrhoeae Neisseria gonorrhoeae - immunology Neisseria gonorrhoeae - pathogenicity Neisseria meningitidis Neisseria meningitidis - classification Neisseria meningitidis - immunology Neisseria meningitidis - pathogenicity Por1A protein Porin Porins - immunology Species Specificity |
| title | The contrasting mechanisms of serum resistance of Neisseria gonorrhoeae and group B Neisseria meningitidis |
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