Monoclonal antibodies against lipopolysaccharide of Chlamydia trachomatis with cross reactivity to human ApoB
Splenocytes obtained from mice immunized with whole purified elementary bodies of Chlamydia trachomatis were used for hybridoma construction. The resulting clones were screened with ELISA using chlamydial lipopolysaccharide (LPS) and full-length human apolipoprotein B (ApoB). One analyzed clone prod...
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| Veröffentlicht in: | Hybridoma (2005) 2011-04, Vol.30 (2), p.131-136 |
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| creator | Petyaev, Ivan M Zigangirova, Nayilia A Tsibezov, Valeriy V Ross, Agnij Bashmakov, Yuriy K |
| description | Splenocytes obtained from mice immunized with whole purified elementary bodies of Chlamydia trachomatis were used for hybridoma construction. The resulting clones were screened with ELISA using chlamydial lipopolysaccharide (LPS) and full-length human apolipoprotein B (ApoB). One analyzed clone producing IgG1 (MAb 7B5) showed simultaneous recognition of chlamydial LPS and human ApoB, suggesting the presence of common antigenic epitopes in their structures. MAb 7B5 exhibited agreeable activity in immunoblot analysis conducted using chlamydial extracts or full-length human ApoB as well as in immunofluorescence (IF) detecting typical inclusion bodies of C. trachomatis and C. pneumoniae in the infected eukaryotic host cells. The removal of LPS from chlamydial suspensions with lauroyl sarcosyl led to a complete disappearance of IF associated with the elementary bodies of C. trachomatis. Therefore, immunologic response to chlamydial antigen may be associated with the generation of ApoB-specific antibody. Molecular mimicry and subsequent formation of cross-reactive antibodies might be an essential mechanism explaining the appearance of circulating auto-antibodies against low density lipoproteins (LDL) in patients with atherosclerosis. Moreover, newly generated MAb 7B5 can be a useful tool in the laboratory diagnosis of chlamydial infections. |
| doi_str_mv | 10.1089/hyb.2010.0107 |
| format | Article |
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The resulting clones were screened with ELISA using chlamydial lipopolysaccharide (LPS) and full-length human apolipoprotein B (ApoB). One analyzed clone producing IgG1 (MAb 7B5) showed simultaneous recognition of chlamydial LPS and human ApoB, suggesting the presence of common antigenic epitopes in their structures. MAb 7B5 exhibited agreeable activity in immunoblot analysis conducted using chlamydial extracts or full-length human ApoB as well as in immunofluorescence (IF) detecting typical inclusion bodies of C. trachomatis and C. pneumoniae in the infected eukaryotic host cells. The removal of LPS from chlamydial suspensions with lauroyl sarcosyl led to a complete disappearance of IF associated with the elementary bodies of C. trachomatis. Therefore, immunologic response to chlamydial antigen may be associated with the generation of ApoB-specific antibody. Molecular mimicry and subsequent formation of cross-reactive antibodies might be an essential mechanism explaining the appearance of circulating auto-antibodies against low density lipoproteins (LDL) in patients with atherosclerosis. Moreover, newly generated MAb 7B5 can be a useful tool in the laboratory diagnosis of chlamydial infections.</description><identifier>ISSN: 1554-0014</identifier><identifier>EISSN: 1557-8348</identifier><identifier>DOI: 10.1089/hyb.2010.0107</identifier><identifier>PMID: 21529285</identifier><language>eng</language><publisher>United States: Mary Ann Liebert, Inc</publisher><subject>Animals ; Antibodies, Bacterial - biosynthesis ; Antibodies, Bacterial - immunology ; Antibodies, Bacterial - isolation & purification ; Antibodies, Monoclonal - biosynthesis ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - isolation & purification ; Antigens, Bacterial - analysis ; Antigens, Bacterial - immunology ; Apolipoproteins B - immunology ; Atherosclerosis - immunology ; Blotting, Western ; Chlamydia Infections - diagnosis ; Chlamydia Infections - immunology ; Chlamydia trachomatis ; Chlamydia trachomatis - chemistry ; Chlamydia trachomatis - immunology ; Chlamydophila pneumoniae ; Cross Reactions - immunology ; Enzyme-Linked Immunosorbent Assay ; Health aspects ; Humans ; Hybridomas - immunology ; Hybridomas - metabolism ; Immunoglobulin G - immunology ; Immunoglobulin G - isolation & purification ; Lipopolysaccharides ; Lipopolysaccharides - immunology ; Mice ; Molecular Mimicry - immunology ; Monoclonal antibodies ; Physiological aspects</subject><ispartof>Hybridoma (2005), 2011-04, Vol.30 (2), p.131-136</ispartof><rights>COPYRIGHT 2011 Mary Ann Liebert, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-d15c3b290e64ee02ff69d8bf5472671b6c7295cbb070000d3d8b156db6aa0af13</citedby><cites>FETCH-LOGICAL-c392t-d15c3b290e64ee02ff69d8bf5472671b6c7295cbb070000d3d8b156db6aa0af13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21529285$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Petyaev, Ivan M</creatorcontrib><creatorcontrib>Zigangirova, Nayilia A</creatorcontrib><creatorcontrib>Tsibezov, Valeriy V</creatorcontrib><creatorcontrib>Ross, Agnij</creatorcontrib><creatorcontrib>Bashmakov, Yuriy K</creatorcontrib><title>Monoclonal antibodies against lipopolysaccharide of Chlamydia trachomatis with cross reactivity to human ApoB</title><title>Hybridoma (2005)</title><addtitle>Hybridoma (Larchmt)</addtitle><description>Splenocytes obtained from mice immunized with whole purified elementary bodies of Chlamydia trachomatis were used for hybridoma construction. The resulting clones were screened with ELISA using chlamydial lipopolysaccharide (LPS) and full-length human apolipoprotein B (ApoB). One analyzed clone producing IgG1 (MAb 7B5) showed simultaneous recognition of chlamydial LPS and human ApoB, suggesting the presence of common antigenic epitopes in their structures. MAb 7B5 exhibited agreeable activity in immunoblot analysis conducted using chlamydial extracts or full-length human ApoB as well as in immunofluorescence (IF) detecting typical inclusion bodies of C. trachomatis and C. pneumoniae in the infected eukaryotic host cells. The removal of LPS from chlamydial suspensions with lauroyl sarcosyl led to a complete disappearance of IF associated with the elementary bodies of C. trachomatis. Therefore, immunologic response to chlamydial antigen may be associated with the generation of ApoB-specific antibody. Molecular mimicry and subsequent formation of cross-reactive antibodies might be an essential mechanism explaining the appearance of circulating auto-antibodies against low density lipoproteins (LDL) in patients with atherosclerosis. Moreover, newly generated MAb 7B5 can be a useful tool in the laboratory diagnosis of chlamydial infections.</description><subject>Animals</subject><subject>Antibodies, Bacterial - biosynthesis</subject><subject>Antibodies, Bacterial - immunology</subject><subject>Antibodies, Bacterial - isolation & purification</subject><subject>Antibodies, Monoclonal - biosynthesis</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - isolation & purification</subject><subject>Antigens, Bacterial - analysis</subject><subject>Antigens, Bacterial - immunology</subject><subject>Apolipoproteins B - immunology</subject><subject>Atherosclerosis - immunology</subject><subject>Blotting, Western</subject><subject>Chlamydia Infections - diagnosis</subject><subject>Chlamydia Infections - immunology</subject><subject>Chlamydia trachomatis</subject><subject>Chlamydia trachomatis - chemistry</subject><subject>Chlamydia trachomatis - immunology</subject><subject>Chlamydophila pneumoniae</subject><subject>Cross Reactions - immunology</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Hybridomas - immunology</subject><subject>Hybridomas - metabolism</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunoglobulin G - isolation & purification</subject><subject>Lipopolysaccharides</subject><subject>Lipopolysaccharides - immunology</subject><subject>Mice</subject><subject>Molecular Mimicry - immunology</subject><subject>Monoclonal antibodies</subject><subject>Physiological aspects</subject><issn>1554-0014</issn><issn>1557-8348</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUuP1SAUgBvjxBlHl24NiQvd9MqjPLq8c-Njkpm40TU5UDrF0FILV9N_L507mpiYgRAO8J0T4KuqVwTvCFbt-2E1O4rLqgz5pLognMtasUY9vY-bGmPSnFfPU_qOMROKymfVOSWctlTxi2q8jVO0IU4QEEzZm9h5lxDcgZ9SRsHPcY5hTWDtAIvvHIo9OgwBxrXzgPICdogjZJ_QL58HZJeYEloc2Ox_-ryiHNFwHGFC-zlevajOegjJvXyYL6tvHz98PXyub758uj7sb2rLWprrjnDLDG2xE41zmPa9aDtlet5IKiQxwkracmsMlri0jpVDwkVnBACGnrDL6u2p7rzEH0eXsh59si4EmFw8Jq1EIxWWbVvId4-ShFGmCOWUF_TNCb2D4LSf-ri9fsP1nnLBBFecFmr3H6r0zo3exsn1vuz_k1CfEu6_bnG9nhc_wrJqgvWmWBfFelOsN8WFf_1w46MZXfeX_uOU_QZo36Ho</recordid><startdate>201104</startdate><enddate>201104</enddate><creator>Petyaev, Ivan M</creator><creator>Zigangirova, Nayilia A</creator><creator>Tsibezov, Valeriy V</creator><creator>Ross, Agnij</creator><creator>Bashmakov, Yuriy K</creator><general>Mary Ann Liebert, Inc</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>201104</creationdate><title>Monoclonal antibodies against lipopolysaccharide of Chlamydia trachomatis with cross reactivity to human ApoB</title><author>Petyaev, Ivan M ; Zigangirova, Nayilia A ; Tsibezov, Valeriy V ; Ross, Agnij ; Bashmakov, Yuriy K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-d15c3b290e64ee02ff69d8bf5472671b6c7295cbb070000d3d8b156db6aa0af13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Antibodies, Bacterial - biosynthesis</topic><topic>Antibodies, Bacterial - immunology</topic><topic>Antibodies, Bacterial - isolation & purification</topic><topic>Antibodies, Monoclonal - biosynthesis</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - isolation & purification</topic><topic>Antigens, Bacterial - analysis</topic><topic>Antigens, Bacterial - immunology</topic><topic>Apolipoproteins B - immunology</topic><topic>Atherosclerosis - immunology</topic><topic>Blotting, Western</topic><topic>Chlamydia Infections - diagnosis</topic><topic>Chlamydia Infections - immunology</topic><topic>Chlamydia trachomatis</topic><topic>Chlamydia trachomatis - chemistry</topic><topic>Chlamydia trachomatis - immunology</topic><topic>Chlamydophila pneumoniae</topic><topic>Cross Reactions - immunology</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Health aspects</topic><topic>Humans</topic><topic>Hybridomas - immunology</topic><topic>Hybridomas - metabolism</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunoglobulin G - isolation & purification</topic><topic>Lipopolysaccharides</topic><topic>Lipopolysaccharides - immunology</topic><topic>Mice</topic><topic>Molecular Mimicry - immunology</topic><topic>Monoclonal antibodies</topic><topic>Physiological aspects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Petyaev, Ivan M</creatorcontrib><creatorcontrib>Zigangirova, Nayilia A</creatorcontrib><creatorcontrib>Tsibezov, Valeriy V</creatorcontrib><creatorcontrib>Ross, Agnij</creatorcontrib><creatorcontrib>Bashmakov, Yuriy K</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>Hybridoma (2005)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Petyaev, Ivan M</au><au>Zigangirova, Nayilia A</au><au>Tsibezov, Valeriy V</au><au>Ross, Agnij</au><au>Bashmakov, Yuriy K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoclonal antibodies against lipopolysaccharide of Chlamydia trachomatis with cross reactivity to human ApoB</atitle><jtitle>Hybridoma (2005)</jtitle><addtitle>Hybridoma (Larchmt)</addtitle><date>2011-04</date><risdate>2011</risdate><volume>30</volume><issue>2</issue><spage>131</spage><epage>136</epage><pages>131-136</pages><issn>1554-0014</issn><eissn>1557-8348</eissn><abstract>Splenocytes obtained from mice immunized with whole purified elementary bodies of Chlamydia trachomatis were used for hybridoma construction. The resulting clones were screened with ELISA using chlamydial lipopolysaccharide (LPS) and full-length human apolipoprotein B (ApoB). One analyzed clone producing IgG1 (MAb 7B5) showed simultaneous recognition of chlamydial LPS and human ApoB, suggesting the presence of common antigenic epitopes in their structures. MAb 7B5 exhibited agreeable activity in immunoblot analysis conducted using chlamydial extracts or full-length human ApoB as well as in immunofluorescence (IF) detecting typical inclusion bodies of C. trachomatis and C. pneumoniae in the infected eukaryotic host cells. The removal of LPS from chlamydial suspensions with lauroyl sarcosyl led to a complete disappearance of IF associated with the elementary bodies of C. trachomatis. Therefore, immunologic response to chlamydial antigen may be associated with the generation of ApoB-specific antibody. Molecular mimicry and subsequent formation of cross-reactive antibodies might be an essential mechanism explaining the appearance of circulating auto-antibodies against low density lipoproteins (LDL) in patients with atherosclerosis. Moreover, newly generated MAb 7B5 can be a useful tool in the laboratory diagnosis of chlamydial infections.</abstract><cop>United States</cop><pub>Mary Ann Liebert, Inc</pub><pmid>21529285</pmid><doi>10.1089/hyb.2010.0107</doi><tpages>6</tpages></addata></record> |
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| subjects | Animals Antibodies, Bacterial - biosynthesis Antibodies, Bacterial - immunology Antibodies, Bacterial - isolation & purification Antibodies, Monoclonal - biosynthesis Antibodies, Monoclonal - immunology Antibodies, Monoclonal - isolation & purification Antigens, Bacterial - analysis Antigens, Bacterial - immunology Apolipoproteins B - immunology Atherosclerosis - immunology Blotting, Western Chlamydia Infections - diagnosis Chlamydia Infections - immunology Chlamydia trachomatis Chlamydia trachomatis - chemistry Chlamydia trachomatis - immunology Chlamydophila pneumoniae Cross Reactions - immunology Enzyme-Linked Immunosorbent Assay Health aspects Humans Hybridomas - immunology Hybridomas - metabolism Immunoglobulin G - immunology Immunoglobulin G - isolation & purification Lipopolysaccharides Lipopolysaccharides - immunology Mice Molecular Mimicry - immunology Monoclonal antibodies Physiological aspects |
| title | Monoclonal antibodies against lipopolysaccharide of Chlamydia trachomatis with cross reactivity to human ApoB |
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