Studies of Structure and Specificity of Some Antigen-Antibody Complexes
By using X-ray diffraction and immunochemical techniques, we have exploited the use of monoclonal antibodies raised against hen egg lysozyme (HEL) to study systematically those factors responsible for the high specificity of antigen-antibody interactions. HEL was chosen for our investigations becaus...
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| Veröffentlicht in: | Philosophical transactions of the Royal Society of London. Series B, Biological sciences Biological sciences, 1989-06, Vol.323 (1217), p.487-494 |
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| creator | Bentley, G. A. Alzari, P. M. Amit, A. G. Boulot, G. Guillon-Chitarra, V. Fischmann, T. Lascombe, M.-b. Mariuzza, R. A. Poljak, R. J. Riottot, M.-m. Saul, F. A. Souchon, H. Tello, D. |
| description | By using X-ray diffraction and immunochemical techniques, we have exploited the use of monoclonal antibodies raised against
hen egg lysozyme (HEL) to study systematically those factors responsible for the high specificity of antigen-antibody interactions.
HEL was chosen for our investigations because its three-dimensional structure and immunochemistry have been well characterized
and because naturally occurring sequence variants from different avian species are readily available to test the fine specificity
of the antibodies. The X-ray crystal structure of a complex formed between HEL and the Fab D1.3 shows a large complementary
surface with close interatomic contacts between antigen and antibody. Thus single amino acid sequence changes in heterologous
antigens give antigen-antibody association constants that are several orders of magnitude smaller than that of the homologous
antigen. For example, a substitution of His for Glu at position 121 in the antigen is sufficient to diminish significantly
the binding between D1.3 and the variant lysozyme. The conformation of HEL when complexed to D1.3 shows no significant difference
from that seen in the free molecule, and immunobinding studies with other anti-HEL antibodies suggest that this observation
may be generally true for the system of monoclonal antibodies that we have studied. |
| doi_str_mv | 10.1098/rstb.1989.0026 |
| format | Article |
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hen egg lysozyme (HEL) to study systematically those factors responsible for the high specificity of antigen-antibody interactions.
HEL was chosen for our investigations because its three-dimensional structure and immunochemistry have been well characterized
and because naturally occurring sequence variants from different avian species are readily available to test the fine specificity
of the antibodies. The X-ray crystal structure of a complex formed between HEL and the Fab D1.3 shows a large complementary
surface with close interatomic contacts between antigen and antibody. Thus single amino acid sequence changes in heterologous
antigens give antigen-antibody association constants that are several orders of magnitude smaller than that of the homologous
antigen. For example, a substitution of His for Glu at position 121 in the antigen is sufficient to diminish significantly
the binding between D1.3 and the variant lysozyme. The conformation of HEL when complexed to D1.3 shows no significant difference
from that seen in the free molecule, and immunobinding studies with other anti-HEL antibodies suggest that this observation
may be generally true for the system of monoclonal antibodies that we have studied.</description><identifier>ISSN: 0962-8436</identifier><identifier>ISSN: 0080-4622</identifier><identifier>EISSN: 1471-2970</identifier><identifier>EISSN: 2054-0280</identifier><identifier>DOI: 10.1098/rstb.1989.0026</identifier><identifier>PMID: 2569206</identifier><identifier>CODEN: PTRBAE</identifier><language>eng</language><publisher>London: The Royal Society</publisher><subject>Antibodies ; Antibody Specificity ; Antigen antibody complex ; Antigen-Antibody Complex - immunology ; Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation ; Antigens ; Biochemistry, Molecular Biology ; Bioinformatics ; Biological and medical sciences ; Biological Physics ; Cellular Biology ; Chemical Sciences ; Computer Science ; Cristallography ; Cross reaction ; Cross Reactions ; Crystal structure ; Epitopes ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Immune system ; Immunoglobulin Fab Fragments ; Immunoglobulin Variable Region ; Immunoglobulins ; Life Sciences ; Molecular immunology ; Molecules ; Monoclonal antibodies ; Muramidase ; Muramidase - immunology ; Physics ; Structural Biology ; X-Ray Diffraction</subject><ispartof>Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1989-06, Vol.323 (1217), p.487-494</ispartof><rights>Copyright 1989 The Royal Society</rights><rights>Scanned images copyright © 2017, Royal Society</rights><rights>1991 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c583t-1a0194f9afbf947d00c94ee35b2a3c0ddf04bb0b6fcfc1b377471bb0c2b368a43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2396872$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2396872$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19292257$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2569206$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://pasteur.hal.science/pasteur-03136459$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bentley, G. A.</creatorcontrib><creatorcontrib>Alzari, P. M.</creatorcontrib><creatorcontrib>Amit, A. G.</creatorcontrib><creatorcontrib>Boulot, G.</creatorcontrib><creatorcontrib>Guillon-Chitarra, V.</creatorcontrib><creatorcontrib>Fischmann, T.</creatorcontrib><creatorcontrib>Lascombe, M.-b.</creatorcontrib><creatorcontrib>Mariuzza, R. A.</creatorcontrib><creatorcontrib>Poljak, R. J.</creatorcontrib><creatorcontrib>Riottot, M.-m.</creatorcontrib><creatorcontrib>Saul, F. A.</creatorcontrib><creatorcontrib>Souchon, H.</creatorcontrib><creatorcontrib>Tello, D.</creatorcontrib><title>Studies of Structure and Specificity of Some Antigen-Antibody Complexes</title><title>Philosophical transactions of the Royal Society of London. Series B, Biological sciences</title><addtitle>Phil. Trans. R. Soc. Lond. B</addtitle><addtitle>Philos Trans R Soc Lond B Biol Sci</addtitle><description>By using X-ray diffraction and immunochemical techniques, we have exploited the use of monoclonal antibodies raised against
hen egg lysozyme (HEL) to study systematically those factors responsible for the high specificity of antigen-antibody interactions.
HEL was chosen for our investigations because its three-dimensional structure and immunochemistry have been well characterized
and because naturally occurring sequence variants from different avian species are readily available to test the fine specificity
of the antibodies. The X-ray crystal structure of a complex formed between HEL and the Fab D1.3 shows a large complementary
surface with close interatomic contacts between antigen and antibody. Thus single amino acid sequence changes in heterologous
antigens give antigen-antibody association constants that are several orders of magnitude smaller than that of the homologous
antigen. For example, a substitution of His for Glu at position 121 in the antigen is sufficient to diminish significantly
the binding between D1.3 and the variant lysozyme. The conformation of HEL when complexed to D1.3 shows no significant difference
from that seen in the free molecule, and immunobinding studies with other anti-HEL antibodies suggest that this observation
may be generally true for the system of monoclonal antibodies that we have studied.</description><subject>Antibodies</subject><subject>Antibody Specificity</subject><subject>Antigen antibody complex</subject><subject>Antigen-Antibody Complex - immunology</subject><subject>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</subject><subject>Antigens</subject><subject>Biochemistry, Molecular Biology</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biological Physics</subject><subject>Cellular Biology</subject><subject>Chemical Sciences</subject><subject>Computer Science</subject><subject>Cristallography</subject><subject>Cross reaction</subject><subject>Cross Reactions</subject><subject>Crystal structure</subject><subject>Epitopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Immune system</subject><subject>Immunoglobulin Fab Fragments</subject><subject>Immunoglobulin Variable Region</subject><subject>Immunoglobulins</subject><subject>Life Sciences</subject><subject>Molecular immunology</subject><subject>Molecules</subject><subject>Monoclonal antibodies</subject><subject>Muramidase</subject><subject>Muramidase - immunology</subject><subject>Physics</subject><subject>Structural Biology</subject><subject>X-Ray Diffraction</subject><issn>0962-8436</issn><issn>0080-4622</issn><issn>1471-2970</issn><issn>2054-0280</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9ksFv0zAUxiMEGmVw5QRSLnBLebaTOD6hUo0NqRISHWfLcezNVRIH2xlkfz1OW22qEDtZ9vu9z9_77CR5i2CJgFWfnA_1ErGKLQFw-SxZoJyiDDMKz5MFsBJnVU7Kl8kr73cAwAqanyVnuCgZhnKRXG7D2BjlU6vTbXCjDKNTqeibdDsoabSRJkz7ou1UuuqDuVF9Nq-1baZ0bbuhVX-Uf5280KL16s1xPU9-fr24Xl9lm--X39arTSaLioQMCUAs10zoWrOcNgCS5UqRosaCSGgaDXldQ11qqSWqCaVxmnggcU3KSuTkPMkOurei5YMznXATt8Lwq9WGD8IHNToOBJEyL9gdivzHAz84-2tUPvDOeKnaVvTKjp5ThnCBKYvg8gBKZ713Sj-oI-Bz0nxOms9J8znp2PD-qDzWnWoe8GO0sf7hWBdeilY70UvjH1UZZhgXNHL-wDk7xeSsNCpMfGdH18ct_7G9_oJYye4IJgZhRDlUBEFRQIH4vRn2tmaAR4Ab70fF99ip3X_dk6du_e_M7w5dOx-sexyZsLKiOJbh-Djm5va3cYqfqMfNEOVmn3uHeTVP__nJlvl-afug-nDSyPXYxg_QaPIX77rukg</recordid><startdate>19890612</startdate><enddate>19890612</enddate><creator>Bentley, G. A.</creator><creator>Alzari, P. M.</creator><creator>Amit, A. G.</creator><creator>Boulot, G.</creator><creator>Guillon-Chitarra, V.</creator><creator>Fischmann, T.</creator><creator>Lascombe, M.-b.</creator><creator>Mariuzza, R. A.</creator><creator>Poljak, R. J.</creator><creator>Riottot, M.-m.</creator><creator>Saul, F. A.</creator><creator>Souchon, H.</creator><creator>Tello, D.</creator><general>The Royal Society</general><general>Royal Society of London</general><general>Royal Society, The</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>7X8</scope><scope>1XC</scope></search><sort><creationdate>19890612</creationdate><title>Studies of Structure and Specificity of Some Antigen-Antibody Complexes</title><author>Bentley, G. A. ; Alzari, P. M. ; Amit, A. G. ; Boulot, G. ; Guillon-Chitarra, V. ; Fischmann, T. ; Lascombe, M.-b. ; Mariuzza, R. A. ; Poljak, R. J. ; Riottot, M.-m. ; Saul, F. A. ; Souchon, H. ; Tello, D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c583t-1a0194f9afbf947d00c94ee35b2a3c0ddf04bb0b6fcfc1b377471bb0c2b368a43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Antibodies</topic><topic>Antibody Specificity</topic><topic>Antigen antibody complex</topic><topic>Antigen-Antibody Complex - immunology</topic><topic>Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation</topic><topic>Antigens</topic><topic>Biochemistry, Molecular Biology</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biological Physics</topic><topic>Cellular Biology</topic><topic>Chemical Sciences</topic><topic>Computer Science</topic><topic>Cristallography</topic><topic>Cross reaction</topic><topic>Cross Reactions</topic><topic>Crystal structure</topic><topic>Epitopes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Immune system</topic><topic>Immunoglobulin Fab Fragments</topic><topic>Immunoglobulin Variable Region</topic><topic>Immunoglobulins</topic><topic>Life Sciences</topic><topic>Molecular immunology</topic><topic>Molecules</topic><topic>Monoclonal antibodies</topic><topic>Muramidase</topic><topic>Muramidase - immunology</topic><topic>Physics</topic><topic>Structural Biology</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bentley, G. A.</creatorcontrib><creatorcontrib>Alzari, P. M.</creatorcontrib><creatorcontrib>Amit, A. G.</creatorcontrib><creatorcontrib>Boulot, G.</creatorcontrib><creatorcontrib>Guillon-Chitarra, V.</creatorcontrib><creatorcontrib>Fischmann, T.</creatorcontrib><creatorcontrib>Lascombe, M.-b.</creatorcontrib><creatorcontrib>Mariuzza, R. A.</creatorcontrib><creatorcontrib>Poljak, R. J.</creatorcontrib><creatorcontrib>Riottot, M.-m.</creatorcontrib><creatorcontrib>Saul, F. A.</creatorcontrib><creatorcontrib>Souchon, H.</creatorcontrib><creatorcontrib>Tello, D.</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>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Philosophical transactions of the Royal Society of London. Series B, Biological sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bentley, G. A.</au><au>Alzari, P. M.</au><au>Amit, A. G.</au><au>Boulot, G.</au><au>Guillon-Chitarra, V.</au><au>Fischmann, T.</au><au>Lascombe, M.-b.</au><au>Mariuzza, R. A.</au><au>Poljak, R. J.</au><au>Riottot, M.-m.</au><au>Saul, F. A.</au><au>Souchon, H.</au><au>Tello, D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies of Structure and Specificity of Some Antigen-Antibody Complexes</atitle><jtitle>Philosophical transactions of the Royal Society of London. Series B, Biological sciences</jtitle><stitle>Phil. Trans. R. Soc. Lond. B</stitle><addtitle>Philos Trans R Soc Lond B Biol Sci</addtitle><date>1989-06-12</date><risdate>1989</risdate><volume>323</volume><issue>1217</issue><spage>487</spage><epage>494</epage><pages>487-494</pages><issn>0962-8436</issn><issn>0080-4622</issn><eissn>1471-2970</eissn><eissn>2054-0280</eissn><coden>PTRBAE</coden><abstract>By using X-ray diffraction and immunochemical techniques, we have exploited the use of monoclonal antibodies raised against
hen egg lysozyme (HEL) to study systematically those factors responsible for the high specificity of antigen-antibody interactions.
HEL was chosen for our investigations because its three-dimensional structure and immunochemistry have been well characterized
and because naturally occurring sequence variants from different avian species are readily available to test the fine specificity
of the antibodies. The X-ray crystal structure of a complex formed between HEL and the Fab D1.3 shows a large complementary
surface with close interatomic contacts between antigen and antibody. Thus single amino acid sequence changes in heterologous
antigens give antigen-antibody association constants that are several orders of magnitude smaller than that of the homologous
antigen. For example, a substitution of His for Glu at position 121 in the antigen is sufficient to diminish significantly
the binding between D1.3 and the variant lysozyme. The conformation of HEL when complexed to D1.3 shows no significant difference
from that seen in the free molecule, and immunobinding studies with other anti-HEL antibodies suggest that this observation
may be generally true for the system of monoclonal antibodies that we have studied.</abstract><cop>London</cop><pub>The Royal Society</pub><pmid>2569206</pmid><doi>10.1098/rstb.1989.0026</doi><tpages>8</tpages></addata></record> |
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| ispartof | Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1989-06, Vol.323 (1217), p.487-494 |
| issn | 0962-8436 0080-4622 1471-2970 2054-0280 |
| language | eng |
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| source | Jstor Complete Legacy; MEDLINE |
| subjects | Antibodies Antibody Specificity Antigen antibody complex Antigen-Antibody Complex - immunology Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation Antigens Biochemistry, Molecular Biology Bioinformatics Biological and medical sciences Biological Physics Cellular Biology Chemical Sciences Computer Science Cristallography Cross reaction Cross Reactions Crystal structure Epitopes Fundamental and applied biological sciences. Psychology Fundamental immunology Immune system Immunoglobulin Fab Fragments Immunoglobulin Variable Region Immunoglobulins Life Sciences Molecular immunology Molecules Monoclonal antibodies Muramidase Muramidase - immunology Physics Structural Biology X-Ray Diffraction |
| title | Studies of Structure and Specificity of Some Antigen-Antibody Complexes |
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