Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies
Monoclonal antibodies (MoAbs) reactive with the authentic Orientia tsutsugamushi 56-kDa protein were generated. MoAb FS10 and FS15 showed in vitro, as well as, in vivo neutralizing activity upon O. tsutsugamushi infection. Deletion mutants of the gene for 56-kDa protein of O. tsutsugamushi Boryong w...
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| Veröffentlicht in: | Vaccine 2000-08, Vol.19 (1), p.2-9 |
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| container_title | Vaccine |
| container_volume | 19 |
| creator | Seong, S.Y. Kim, M.K. Lee, S.M. Odgerel, Z. Choi, M.S. Han, T.H. Kim, I.S. Kang, J.S. Lim, B.U. |
| description | Monoclonal antibodies (MoAbs) reactive with the authentic
Orientia tsutsugamushi 56-kDa protein were generated. MoAb FS10 and FS15 showed in vitro, as well as, in vivo neutralizing activity upon
O. tsutsugamushi infection. Deletion mutants of the gene for 56-kDa protein of
O. tsutsugamushi Boryong were expressed to map the binding region. FS10 and FS15 are bound to amino acids (aa) located in an antigenic domain II, at residues 140–160 and 187–214, respectively. Computer modeling indicated that aa 146–153 were important for antigenicity against FS10. A sequence for aa 142–150 was highly homologous between oriential strains. These results suggest that the antigenic determinant for neutralizing MoAbs is an epitope within aa 140–160. Furthermore, this region may be important for the adhesion/invasion or intracellular survival of
O. tsutsugamushi within host cells. |
| doi_str_mv | 10.1016/S0264-410X(00)00167-5 |
| format | Article |
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Orientia tsutsugamushi 56-kDa protein were generated. MoAb FS10 and FS15 showed in vitro, as well as, in vivo neutralizing activity upon
O. tsutsugamushi infection. Deletion mutants of the gene for 56-kDa protein of
O. tsutsugamushi Boryong were expressed to map the binding region. FS10 and FS15 are bound to amino acids (aa) located in an antigenic domain II, at residues 140–160 and 187–214, respectively. Computer modeling indicated that aa 146–153 were important for antigenicity against FS10. A sequence for aa 142–150 was highly homologous between oriential strains. These results suggest that the antigenic determinant for neutralizing MoAbs is an epitope within aa 140–160. Furthermore, this region may be important for the adhesion/invasion or intracellular survival of
O. tsutsugamushi within host cells.</description><identifier>ISSN: 0264-410X</identifier><identifier>EISSN: 1873-2518</identifier><identifier>DOI: 10.1016/S0264-410X(00)00167-5</identifier><identifier>PMID: 10924780</identifier><identifier>CODEN: VACCDE</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>56-kDa protein ; Amino Acid Sequence ; Animals ; Antibodies, Bacterial - immunology ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - therapeutic use ; Bacteriology ; Biological and medical sciences ; Disease Models, Animal ; Epitope Mapping ; Epitopes - immunology ; Fundamental and applied biological sciences. Psychology ; Mice ; Mice, Inbred BALB C ; Microbiology ; Molecular Sequence Data ; Molecular Weight ; Neutralization ; Neutralization Tests ; Orientia tsutsugamushi ; Orientia tsutsugamushi - immunology ; Scrub Typhus - immunology ; Scrub Typhus - mortality ; Scrub Typhus - prevention & control ; Sequence Homology, Amino Acid ; Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies</subject><ispartof>Vaccine, 2000-08, Vol.19 (1), p.2-9</ispartof><rights>2000 Elsevier Science Ltd</rights><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c516t-14dc68d09ca9bc199698bfb6041869c67e130daa7ce6745fbacd106b3a6bece03</citedby><cites>FETCH-LOGICAL-c516t-14dc68d09ca9bc199698bfb6041869c67e130daa7ce6745fbacd106b3a6bece03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0264-410X(00)00167-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976,64366</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1480601$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10924780$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Seong, S.Y.</creatorcontrib><creatorcontrib>Kim, M.K.</creatorcontrib><creatorcontrib>Lee, S.M.</creatorcontrib><creatorcontrib>Odgerel, Z.</creatorcontrib><creatorcontrib>Choi, M.S.</creatorcontrib><creatorcontrib>Han, T.H.</creatorcontrib><creatorcontrib>Kim, I.S.</creatorcontrib><creatorcontrib>Kang, J.S.</creatorcontrib><creatorcontrib>Lim, B.U.</creatorcontrib><title>Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies</title><title>Vaccine</title><addtitle>Vaccine</addtitle><description>Monoclonal antibodies (MoAbs) reactive with the authentic
Orientia tsutsugamushi 56-kDa protein were generated. MoAb FS10 and FS15 showed in vitro, as well as, in vivo neutralizing activity upon
O. tsutsugamushi infection. Deletion mutants of the gene for 56-kDa protein of
O. tsutsugamushi Boryong were expressed to map the binding region. FS10 and FS15 are bound to amino acids (aa) located in an antigenic domain II, at residues 140–160 and 187–214, respectively. Computer modeling indicated that aa 146–153 were important for antigenicity against FS10. A sequence for aa 142–150 was highly homologous between oriential strains. These results suggest that the antigenic determinant for neutralizing MoAbs is an epitope within aa 140–160. Furthermore, this region may be important for the adhesion/invasion or intracellular survival of
O. tsutsugamushi within host cells.</description><subject>56-kDa protein</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Bacterial - immunology</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - therapeutic use</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Disease Models, Animal</subject><subject>Epitope Mapping</subject><subject>Epitopes - immunology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Neutralization</subject><subject>Neutralization Tests</subject><subject>Orientia tsutsugamushi</subject><subject>Orientia tsutsugamushi - immunology</subject><subject>Scrub Typhus - immunology</subject><subject>Scrub Typhus - mortality</subject><subject>Scrub Typhus - prevention & control</subject><subject>Sequence Homology, Amino Acid</subject><subject>Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies</subject><issn>0264-410X</issn><issn>1873-2518</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFDEQgIMo7rj6E5QcRPTQWpnupDsnkfU1sLgHFbyF6qR6N9rdGZP0wnrzn5t5oN4WAglVX6qK-hh7LOClAKFefYa1aqpGwLfnAC-ghNpK3mEr0bV1tZaiu8tWf5ET9iCl7wAga6HvsxMBet20HazY70-05Iij_4XZh5nT1uewpcTLO18Rxzn7S5q95S5M6Ge-2fAw7FMX0VPJIs9pKecSpyVdeS5V9eMt8m0MmQof6ZpwJMf7Gz6FOdgxzDju6_bBeUoP2b0Bx0SPjvcp-_r-3Zezj9X5xYfN2ZvzykqhciUaZ1XnQFvUvRVaK931Q6-gEZ3SVrUkanCIrSXVNnLo0ToBqq9R9WQJ6lP27FC3TPZzoZTN5JOlccSZwpJMK9pGy7Kh20DRKqGl2lWUB9DGkFKkwWyjnzDeGAFmJ8nsJZmdAQNg9pLMrsGTY4Oln8j99-tgpQBPjwAmi-MQcbY-_eOaDhSIgr0-YFTWdu0pmmSLEkvOR7LZuOBvmeQPiGGwpg</recordid><startdate>20000815</startdate><enddate>20000815</enddate><creator>Seong, S.Y.</creator><creator>Kim, M.K.</creator><creator>Lee, S.M.</creator><creator>Odgerel, Z.</creator><creator>Choi, M.S.</creator><creator>Han, T.H.</creator><creator>Kim, I.S.</creator><creator>Kang, J.S.</creator><creator>Lim, B.U.</creator><general>Elsevier Ltd</general><general>Elsevier</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>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20000815</creationdate><title>Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies</title><author>Seong, S.Y. ; Kim, M.K. ; Lee, S.M. ; Odgerel, Z. ; Choi, M.S. ; Han, T.H. ; Kim, I.S. ; Kang, J.S. ; Lim, B.U.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c516t-14dc68d09ca9bc199698bfb6041869c67e130daa7ce6745fbacd106b3a6bece03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>56-kDa protein</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Bacterial - immunology</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - therapeutic use</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Disease Models, Animal</topic><topic>Epitope Mapping</topic><topic>Epitopes - immunology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Neutralization</topic><topic>Neutralization Tests</topic><topic>Orientia tsutsugamushi</topic><topic>Orientia tsutsugamushi - immunology</topic><topic>Scrub Typhus - immunology</topic><topic>Scrub Typhus - mortality</topic><topic>Scrub Typhus - prevention & control</topic><topic>Sequence Homology, Amino Acid</topic><topic>Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Seong, S.Y.</creatorcontrib><creatorcontrib>Kim, M.K.</creatorcontrib><creatorcontrib>Lee, S.M.</creatorcontrib><creatorcontrib>Odgerel, Z.</creatorcontrib><creatorcontrib>Choi, M.S.</creatorcontrib><creatorcontrib>Han, T.H.</creatorcontrib><creatorcontrib>Kim, I.S.</creatorcontrib><creatorcontrib>Kang, J.S.</creatorcontrib><creatorcontrib>Lim, B.U.</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>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>Vaccine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Seong, S.Y.</au><au>Kim, M.K.</au><au>Lee, S.M.</au><au>Odgerel, Z.</au><au>Choi, M.S.</au><au>Han, T.H.</au><au>Kim, I.S.</au><au>Kang, J.S.</au><au>Lim, B.U.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies</atitle><jtitle>Vaccine</jtitle><addtitle>Vaccine</addtitle><date>2000-08-15</date><risdate>2000</risdate><volume>19</volume><issue>1</issue><spage>2</spage><epage>9</epage><pages>2-9</pages><issn>0264-410X</issn><eissn>1873-2518</eissn><coden>VACCDE</coden><abstract>Monoclonal antibodies (MoAbs) reactive with the authentic
Orientia tsutsugamushi 56-kDa protein were generated. MoAb FS10 and FS15 showed in vitro, as well as, in vivo neutralizing activity upon
O. tsutsugamushi infection. Deletion mutants of the gene for 56-kDa protein of
O. tsutsugamushi Boryong were expressed to map the binding region. FS10 and FS15 are bound to amino acids (aa) located in an antigenic domain II, at residues 140–160 and 187–214, respectively. Computer modeling indicated that aa 146–153 were important for antigenicity against FS10. A sequence for aa 142–150 was highly homologous between oriential strains. These results suggest that the antigenic determinant for neutralizing MoAbs is an epitope within aa 140–160. Furthermore, this region may be important for the adhesion/invasion or intracellular survival of
O. tsutsugamushi within host cells.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>10924780</pmid><doi>10.1016/S0264-410X(00)00167-5</doi><tpages>8</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; ProQuest Central UK/Ireland |
| subjects | 56-kDa protein Amino Acid Sequence Animals Antibodies, Bacterial - immunology Antibodies, Monoclonal - immunology Antibodies, Monoclonal - therapeutic use Bacteriology Biological and medical sciences Disease Models, Animal Epitope Mapping Epitopes - immunology Fundamental and applied biological sciences. Psychology Mice Mice, Inbred BALB C Microbiology Molecular Sequence Data Molecular Weight Neutralization Neutralization Tests Orientia tsutsugamushi Orientia tsutsugamushi - immunology Scrub Typhus - immunology Scrub Typhus - mortality Scrub Typhus - prevention & control Sequence Homology, Amino Acid Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies |
| title | Neutralization epitopes on the antigenic domain II of the Orientia tsutsugamushi 56-kDa protein revealed by monoclonal antibodies |
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