Complement Processing and Immunoglobulin Binding to Neisseria gonorrhoeae Determined In Vitro Simulates In Vivo Effects
Local inflammation elicited by Neisseria gonorrhoeae correlates closely with sensitivity to killing by normal human serum. Serum-sensitive (SS) isolates are rendered resistant in vitro by lipooligosaccharide sialylation. Differences in C3b processing on N. gonorrhoeae in vitro were found to match fi...
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| Veröffentlicht in: | The Journal of infectious diseases 1999-01, Vol.179 (1), p.124-135 |
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| container_title | The Journal of infectious diseases |
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| creator | McQuillen, Daniel P. Gulati, Sunita Ram, Sanjay Turner, Adrian K. Jani, Darshana B. Heeren, Timothy C. Rice, Peter A. |
| description | Local inflammation elicited by Neisseria gonorrhoeae correlates closely with sensitivity to killing by normal human serum. Serum-sensitive (SS) isolates are rendered resistant in vitro by lipooligosaccharide sialylation. Differences in C3b processing on N. gonorrhoeae in vitro were found to match findings at the cervical level in vivo. Nonsialylated SS gonococci bound 5-fold more C3b than did stably serum-resistant (SR) gonococci; most was processed to iC3b, yet significant C3b persisted. Sialylated SS gonococci bound 4-fold less total C3 antigen than did SR gonococci, which was promptly converted to iC3b. C3b bound later on stably SR gonococci but again was processed swiftly to iC3b. In vivo, the iC3b/C3 ratio of SS isolates more closely resembled nonsialylated SS isolates in vitro, implying heterogeneous sialylation or desialylation in vivo. In vitro, total IgM bound was unchanged by sialylation of SS isolates, but total C4 bound decreased by 75%, suggesting that sialylation may indirectly regulate the classical complement pathway. |
| doi_str_mv | 10.1086/314545 |
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Serum-sensitive (SS) isolates are rendered resistant in vitro by lipooligosaccharide sialylation. Differences in C3b processing on N. gonorrhoeae in vitro were found to match findings at the cervical level in vivo. Nonsialylated SS gonococci bound 5-fold more C3b than did stably serum-resistant (SR) gonococci; most was processed to iC3b, yet significant C3b persisted. Sialylated SS gonococci bound 4-fold less total C3 antigen than did SR gonococci, which was promptly converted to iC3b. C3b bound later on stably SR gonococci but again was processed swiftly to iC3b. In vivo, the iC3b/C3 ratio of SS isolates more closely resembled nonsialylated SS isolates in vitro, implying heterogeneous sialylation or desialylation in vivo. In vitro, total IgM bound was unchanged by sialylation of SS isolates, but total C4 bound decreased by 75%, suggesting that sialylation may indirectly regulate the classical complement pathway.</description><identifier>ISSN: 0022-1899</identifier><identifier>EISSN: 1537-6613</identifier><identifier>DOI: 10.1086/314545</identifier><identifier>PMID: 9841831</identifier><identifier>CODEN: JIDIAQ</identifier><language>eng</language><publisher>Chicago, IL: University Chicago Press</publisher><subject>Animals ; Antibodies, Monoclonal ; Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. 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Psychology ; Fundamental immunology ; Gonorrhea - etiology ; Gonorrhea - immunology ; Gonorrhea - microbiology ; Human bacterial diseases ; Humans ; Immunoglobulins ; Immunoglobulins - metabolism ; In Vitro Techniques ; Infections ; Infectious diseases ; Kinetics ; Lipopolysaccharides - chemistry ; Lipopolysaccharides - immunology ; Major Articles ; Medical sciences ; Methylamines ; Mice ; Molecular immunology ; Molecules ; Monoclonal antibodies ; Neisseria gonorrhoeae ; Neisseria gonorrhoeae - immunology ; Neisseria gonorrhoeae - isolation & purification ; Neisseria gonorrhoeae - pathogenicity ; Sialic Acids - chemistry</subject><ispartof>The Journal of infectious diseases, 1999-01, Vol.179 (1), p.124-135</ispartof><rights>Copyright 1999 Infectious Diseases Society of America</rights><rights>1999 INIST-CNRS</rights><rights>Copyright University of Chicago, acting through its Press Jan 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-58dd21e2f2dfdc9350ac5ff6bf6828669d781eb24c8ab7d22e55d46dc57c08223</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30117235$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30117235$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,4024,27923,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1636350$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9841831$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McQuillen, Daniel P.</creatorcontrib><creatorcontrib>Gulati, Sunita</creatorcontrib><creatorcontrib>Ram, Sanjay</creatorcontrib><creatorcontrib>Turner, Adrian K.</creatorcontrib><creatorcontrib>Jani, Darshana B.</creatorcontrib><creatorcontrib>Heeren, Timothy C.</creatorcontrib><creatorcontrib>Rice, Peter A.</creatorcontrib><title>Complement Processing and Immunoglobulin Binding to Neisseria gonorrhoeae Determined In Vitro Simulates In Vivo Effects</title><title>The Journal of infectious diseases</title><addtitle>The Journal of Infectious Diseases</addtitle><description>Local inflammation elicited by Neisseria gonorrhoeae correlates closely with sensitivity to killing by normal human serum. Serum-sensitive (SS) isolates are rendered resistant in vitro by lipooligosaccharide sialylation. Differences in C3b processing on N. gonorrhoeae in vitro were found to match findings at the cervical level in vivo. Nonsialylated SS gonococci bound 5-fold more C3b than did stably serum-resistant (SR) gonococci; most was processed to iC3b, yet significant C3b persisted. Sialylated SS gonococci bound 4-fold less total C3 antigen than did SR gonococci, which was promptly converted to iC3b. C3b bound later on stably SR gonococci but again was processed swiftly to iC3b. In vivo, the iC3b/C3 ratio of SS isolates more closely resembled nonsialylated SS isolates in vitro, implying heterogeneous sialylation or desialylation in vivo. In vitro, total IgM bound was unchanged by sialylation of SS isolates, but total C4 bound decreased by 75%, suggesting that sialylation may indirectly regulate the classical complement pathway.</description><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</subject><subject>Antigens</subject><subject>Bacterial diseases</subject><subject>Bacterial diseases of the genital system</subject><subject>Biological and medical sciences</subject><subject>Blood Bactericidal Activity - immunology</subject><subject>Cervical vertebrae</subject><subject>Complement C3b - metabolism</subject><subject>Complement Factor B - metabolism</subject><subject>Complement Pathway, Alternative</subject><subject>Complement Pathway, Classical</subject><subject>Complement System Proteins - metabolism</subject><subject>Enzyme linked immunosorbent assay</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Gonorrhea - etiology</subject><subject>Gonorrhea - immunology</subject><subject>Gonorrhea - microbiology</subject><subject>Human bacterial diseases</subject><subject>Humans</subject><subject>Immunoglobulins</subject><subject>Immunoglobulins - metabolism</subject><subject>In Vitro Techniques</subject><subject>Infections</subject><subject>Infectious diseases</subject><subject>Kinetics</subject><subject>Lipopolysaccharides - chemistry</subject><subject>Lipopolysaccharides - immunology</subject><subject>Major Articles</subject><subject>Medical sciences</subject><subject>Methylamines</subject><subject>Mice</subject><subject>Molecular immunology</subject><subject>Molecules</subject><subject>Monoclonal antibodies</subject><subject>Neisseria gonorrhoeae</subject><subject>Neisseria gonorrhoeae - immunology</subject><subject>Neisseria gonorrhoeae - isolation & purification</subject><subject>Neisseria gonorrhoeae - pathogenicity</subject><subject>Sialic Acids - chemistry</subject><issn>0022-1899</issn><issn>1537-6613</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkd1uEzEQRlcIVNICb4BkIcTdgn_WXu8lDQ0tigAJKBU3lmOPg8OuHWwvhbdno0Qp4srSnG-Ox56qekLwS4KleMVIwxt-r5oRztpaCMLuVzOMKa2J7LqH1WnOG4xxw0R7Up10siGSkVl1O4_DtocBQkEfUzSQsw9rpINFV8Mwhrju42rsfUDnPtgdKhG9B58zJK_ROoaY0vcIGtAbKJAGH2BqDejalxTRJz-MvS6Q96VfEV04B6bkR9UDp_sMjw_nWfVlcfF5flkvP7y9mr9e1oZ1uNRcWksJUEets6ZjHGvDnRMrJySVQnS2lQRWtDFSr1pLKXBuG2ENbw2WlLKz6sXeu03x5wi5qMFnA32vA8QxK9HxRnRCTMFn_wU3cUxhmk1Nmg6LFv9jMynmnMCpbfKDTn8UwWq3BrVfwxR8erCNqwHsMXb494k_P3Cdje5d0sH4fGcTTExvvdNsconpiBkmpKVsd0295z4X-H3kOv1QomUtV5c339QCX7N3Xxc3asn-Ao3fp84</recordid><startdate>199901</startdate><enddate>199901</enddate><creator>McQuillen, Daniel P.</creator><creator>Gulati, Sunita</creator><creator>Ram, Sanjay</creator><creator>Turner, Adrian K.</creator><creator>Jani, Darshana B.</creator><creator>Heeren, Timothy C.</creator><creator>Rice, Peter A.</creator><general>University Chicago Press</general><general>University of Chicago Press</general><general>Oxford University Press</general><scope>BSCLL</scope><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>K9.</scope><scope>NAPCQ</scope><scope>7X8</scope></search><sort><creationdate>199901</creationdate><title>Complement Processing and Immunoglobulin Binding to Neisseria gonorrhoeae Determined In Vitro Simulates In Vivo Effects</title><author>McQuillen, Daniel P. ; Gulati, Sunita ; Ram, Sanjay ; Turner, Adrian K. ; Jani, Darshana B. ; Heeren, Timothy C. ; Rice, Peter A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390t-58dd21e2f2dfdc9350ac5ff6bf6828669d781eb24c8ab7d22e55d46dc57c08223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</topic><topic>Antigens</topic><topic>Bacterial diseases</topic><topic>Bacterial diseases of the genital system</topic><topic>Biological and medical sciences</topic><topic>Blood Bactericidal Activity - immunology</topic><topic>Cervical vertebrae</topic><topic>Complement C3b - metabolism</topic><topic>Complement Factor B - metabolism</topic><topic>Complement Pathway, Alternative</topic><topic>Complement Pathway, Classical</topic><topic>Complement System Proteins - metabolism</topic><topic>Enzyme linked immunosorbent assay</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Gonorrhea - etiology</topic><topic>Gonorrhea - immunology</topic><topic>Gonorrhea - microbiology</topic><topic>Human bacterial diseases</topic><topic>Humans</topic><topic>Immunoglobulins</topic><topic>Immunoglobulins - metabolism</topic><topic>In Vitro Techniques</topic><topic>Infections</topic><topic>Infectious diseases</topic><topic>Kinetics</topic><topic>Lipopolysaccharides - chemistry</topic><topic>Lipopolysaccharides - immunology</topic><topic>Major Articles</topic><topic>Medical sciences</topic><topic>Methylamines</topic><topic>Mice</topic><topic>Molecular immunology</topic><topic>Molecules</topic><topic>Monoclonal antibodies</topic><topic>Neisseria gonorrhoeae</topic><topic>Neisseria gonorrhoeae - immunology</topic><topic>Neisseria gonorrhoeae - isolation & purification</topic><topic>Neisseria gonorrhoeae - pathogenicity</topic><topic>Sialic Acids - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McQuillen, Daniel P.</creatorcontrib><creatorcontrib>Gulati, Sunita</creatorcontrib><creatorcontrib>Ram, Sanjay</creatorcontrib><creatorcontrib>Turner, Adrian K.</creatorcontrib><creatorcontrib>Jani, Darshana B.</creatorcontrib><creatorcontrib>Heeren, Timothy C.</creatorcontrib><creatorcontrib>Rice, Peter A.</creatorcontrib><collection>Istex</collection><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 Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Premium</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of infectious diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McQuillen, Daniel P.</au><au>Gulati, Sunita</au><au>Ram, Sanjay</au><au>Turner, Adrian K.</au><au>Jani, Darshana B.</au><au>Heeren, Timothy C.</au><au>Rice, Peter A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complement Processing and Immunoglobulin Binding to Neisseria gonorrhoeae Determined In Vitro Simulates In Vivo Effects</atitle><jtitle>The Journal of infectious diseases</jtitle><addtitle>The Journal of Infectious Diseases</addtitle><date>1999-01</date><risdate>1999</risdate><volume>179</volume><issue>1</issue><spage>124</spage><epage>135</epage><pages>124-135</pages><issn>0022-1899</issn><eissn>1537-6613</eissn><coden>JIDIAQ</coden><abstract>Local inflammation elicited by Neisseria gonorrhoeae correlates closely with sensitivity to killing by normal human serum. Serum-sensitive (SS) isolates are rendered resistant in vitro by lipooligosaccharide sialylation. Differences in C3b processing on N. gonorrhoeae in vitro were found to match findings at the cervical level in vivo. Nonsialylated SS gonococci bound 5-fold more C3b than did stably serum-resistant (SR) gonococci; most was processed to iC3b, yet significant C3b persisted. Sialylated SS gonococci bound 4-fold less total C3 antigen than did SR gonococci, which was promptly converted to iC3b. C3b bound later on stably SR gonococci but again was processed swiftly to iC3b. In vivo, the iC3b/C3 ratio of SS isolates more closely resembled nonsialylated SS isolates in vitro, implying heterogeneous sialylation or desialylation in vivo. In vitro, total IgM bound was unchanged by sialylation of SS isolates, but total C4 bound decreased by 75%, suggesting that sialylation may indirectly regulate the classical complement pathway.</abstract><cop>Chicago, IL</cop><pub>University Chicago Press</pub><pmid>9841831</pmid><doi>10.1086/314545</doi><tpages>12</tpages></addata></record> |
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| subjects | Animals Antibodies, Monoclonal Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation Antigens Bacterial diseases Bacterial diseases of the genital system Biological and medical sciences Blood Bactericidal Activity - immunology Cervical vertebrae Complement C3b - metabolism Complement Factor B - metabolism Complement Pathway, Alternative Complement Pathway, Classical Complement System Proteins - metabolism Enzyme linked immunosorbent assay Female Fundamental and applied biological sciences. Psychology Fundamental immunology Gonorrhea - etiology Gonorrhea - immunology Gonorrhea - microbiology Human bacterial diseases Humans Immunoglobulins Immunoglobulins - metabolism In Vitro Techniques Infections Infectious diseases Kinetics Lipopolysaccharides - chemistry Lipopolysaccharides - immunology Major Articles Medical sciences Methylamines Mice Molecular immunology Molecules Monoclonal antibodies Neisseria gonorrhoeae Neisseria gonorrhoeae - immunology Neisseria gonorrhoeae - isolation & purification Neisseria gonorrhoeae - pathogenicity Sialic Acids - chemistry |
| title | Complement Processing and Immunoglobulin Binding to Neisseria gonorrhoeae Determined In Vitro Simulates In Vivo Effects |
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