Changes in rheumatoid factor and monoclonal IgG antibody specificity after site-specific mutations in antigenic region of beta 2-microglobulin.
Identifieur interne : 002750 ( PubMed/Checkpoint ); précédent : 002749; suivant : 002751Changes in rheumatoid factor and monoclonal IgG antibody specificity after site-specific mutations in antigenic region of beta 2-microglobulin.
Auteurs : W G Van Eyndhoven ; C C Malone ; R C WilliamsSource :
- Clinical immunology and immunopathology [ 0090-1229 ] ; 1994.
Descripteurs français
- KwdFr :
- Animaux, Anticorps monoclonaux (immunologie), Données de séquences moléculaires, Facteur rhumatoïde (immunologie), Humains, Immunoglobuline G (immunologie), Immunoglobuline M (immunologie), Mutagenèse dirigée (génétique), Polyarthrite rhumatoïde (immunologie), Souris, Spécificité des anticorps, Séquence d'acides aminés, Séquence nucléotidique, Test ELISA, bêta-2-Microglobuline (génétique), bêta-2-Microglobuline (immunologie).
- MESH :
- génétique : Mutagenèse dirigée, bêta-2-Microglobuline.
- immunologie : Anticorps monoclonaux, Facteur rhumatoïde, Immunoglobuline G, Immunoglobuline M, Polyarthrite rhumatoïde, bêta-2-Microglobuline.
- Animaux, Données de séquences moléculaires, Humains, Souris, Spécificité des anticorps, Séquence d'acides aminés, Séquence nucléotidique, Test ELISA.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal (immunology), Antibody Specificity, Arthritis, Rheumatoid (immunology), Base Sequence, Enzyme-Linked Immunosorbent Assay, Humans, Immunoglobulin G (immunology), Immunoglobulin M (immunology), Mice, Molecular Sequence Data, Mutagenesis, Site-Directed (genetics), Rheumatoid Factor (immunology), beta 2-Microglobulin (genetics), beta 2-Microglobulin (immunology).
- MESH :
- chemical , genetics : beta 2-Microglobulin.
- chemical , immunology : Antibodies, Monoclonal, Immunoglobulin G, Immunoglobulin M, Rheumatoid Factor, beta 2-Microglobulin.
- genetics : Mutagenesis, Site-Directed.
- immunology : Arthritis, Rheumatoid.
- Amino Acid Sequence, Animals, Antibody Specificity, Base Sequence, Enzyme-Linked Immunosorbent Assay, Humans, Mice, Molecular Sequence Data.
Abstract
Antigenic epitopes on the SKDWSFY region (positions 57-63) of human beta 2-microglobulin (beta 2m) reacting in ELISA with polyclonal and monoclonal human IgM rheumatoid factors (RF) as well as with monoclonal mouse IgG anti-beta 2m antibodies were studied after site-specific mutation of single or double beta 2m amino acid residues. Single site-specific mutations at lysine 58 and serine 61 produced a major decrease (50-100%) in reactivity of polyclonal IgM RF with beta 2m. Mutations at serine 57, tryptophane 60, and phenylalanine 62 also induced substantial decrements (25-49%) in IgM RF reactivity. beta 2m mutants containing double amino acid mutations including one residue outside the SKDWSFY region along with four different mutations at tryptophane 60 also often showed marked decrements in IgM RF anti-beta 2m reactivity. Site-specific mutations at virtually all residues within the SKDWSFY beta 2m region produced a major decrease in reactivity of two of three monoclonal human IgM RF. Results with nine murine IgG anti-beta 2m mAbs often showed an entirely different profile. Site-specific mutation of aspartic acid at position 59 produced a 50-100% decrease in binding of nine mAbs. Serine at position 61 and tyrosine at 63 also appeared to represent important residues for antigenic determinants reacting with anti-beta 2m mAbs. Results of mapping discrete epitopes using glycine substitution within overlapping 7-mers of beta 2m linear sequence compared with site-specific mutation of single beta 2m residues were similar in many instances, but also often showed marked differences. A marked change in antigenic contribution of single amino acid residues to beta 2m antigenic epitopes frequently depended on what residues were mutated to. Our findings emphasize that single residues within a small seven amino acid, solvent-accessible antigenic stretch of primary beta 2m sequence vary considerably in their contribution to the reactive antigenic structures for IgM RF as well as monoclonal IgG antibodies.
DOI: 10.1006/clin.1994.1154
PubMed: 8062449
Affiliations:
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32610.</nlm:affiliation><wicri:noCountry code="subField">Gainesville 32610</wicri:noCountry></affiliation></author><author><name sortKey="Malone, C C" sort="Malone, C C" uniqKey="Malone C" first="C C" last="Malone">C C Malone</name></author><author><name sortKey="Williams, R C" sort="Williams, R C" uniqKey="Williams R" first="R C" last="Williams">R C Williams</name></author></analytic><series><title level="j">Clinical immunology and immunopathology</title><idno type="ISSN">0090-1229</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibodies, Monoclonal (immunology)</term><term>Antibody Specificity</term><term>Arthritis, Rheumatoid (immunology)</term><term>Base Sequence</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Humans</term><term>Immunoglobulin G (immunology)</term><term>Immunoglobulin M (immunology)</term><term>Mice</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed (genetics)</term><term>Rheumatoid Factor (immunology)</term><term>beta 2-Microglobulin (genetics)</term><term>beta 2-Microglobulin (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps monoclonaux (immunologie)</term><term>Données de séquences moléculaires</term><term>Facteur rhumatoïde (immunologie)</term><term>Humains</term><term>Immunoglobuline G (immunologie)</term><term>Immunoglobuline M (immunologie)</term><term>Mutagenèse dirigée (génétique)</term><term>Polyarthrite rhumatoïde (immunologie)</term><term>Souris</term><term>Spécificité des anticorps</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Test ELISA</term><term>bêta-2-Microglobuline (génétique)</term><term>bêta-2-Microglobuline (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>beta 2-Microglobulin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Immunoglobulin G</term><term>Immunoglobulin M</term><term>Rheumatoid Factor</term><term>beta 2-Microglobulin</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutagenesis, Site-Directed</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutagenèse dirigée</term><term>bêta-2-Microglobuline</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Facteur rhumatoïde</term><term>Immunoglobuline G</term><term>Immunoglobuline M</term><term>Polyarthrite rhumatoïde</term><term>bêta-2-Microglobuline</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Arthritis, Rheumatoid</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibody Specificity</term><term>Base Sequence</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Humans</term><term>Mice</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Souris</term><term>Spécificité des anticorps</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Test ELISA</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Antigenic epitopes on the SKDWSFY region (positions 57-63) of human beta 2-microglobulin (beta 2m) reacting in ELISA with polyclonal and monoclonal human IgM rheumatoid factors (RF) as well as with monoclonal mouse IgG anti-beta 2m antibodies were studied after site-specific mutation of single or double beta 2m amino acid residues. Single site-specific mutations at lysine 58 and serine 61 produced a major decrease (50-100%) in reactivity of polyclonal IgM RF with beta 2m. Mutations at serine 57, tryptophane 60, and phenylalanine 62 also induced substantial decrements (25-49%) in IgM RF reactivity. beta 2m mutants containing double amino acid mutations including one residue outside the SKDWSFY region along with four different mutations at tryptophane 60 also often showed marked decrements in IgM RF anti-beta 2m reactivity. Site-specific mutations at virtually all residues within the SKDWSFY beta 2m region produced a major decrease in reactivity of two of three monoclonal human IgM RF. Results with nine murine IgG anti-beta 2m mAbs often showed an entirely different profile. Site-specific mutation of aspartic acid at position 59 produced a 50-100% decrease in binding of nine mAbs. Serine at position 61 and tyrosine at 63 also appeared to represent important residues for antigenic determinants reacting with anti-beta 2m mAbs. Results of mapping discrete epitopes using glycine substitution within overlapping 7-mers of beta 2m linear sequence compared with site-specific mutation of single beta 2m residues were similar in many instances, but also often showed marked differences. A marked change in antigenic contribution of single amino acid residues to beta 2m antigenic epitopes frequently depended on what residues were mutated to. Our findings emphasize that single residues within a small seven amino acid, solvent-accessible antigenic stretch of primary beta 2m sequence vary considerably in their contribution to the reactive antigenic structures for IgM RF as well as monoclonal IgG antibodies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8062449</PMID><DateCompleted><Year>1994</Year><Month>09</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0090-1229</ISSN><JournalIssue CitedMedium="Print"><Volume>72</Volume><Issue>3</Issue><PubDate><Year>1994</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Clinical immunology and immunopathology</Title><ISOAbbreviation>Clin. Immunol. Immunopathol.</ISOAbbreviation></Journal><ArticleTitle>Changes in rheumatoid factor and monoclonal IgG antibody specificity after site-specific mutations in antigenic region of beta 2-microglobulin.</ArticleTitle><Pagination><MedlinePgn>362-72</MedlinePgn></Pagination><Abstract><AbstractText>Antigenic epitopes on the SKDWSFY region (positions 57-63) of human beta 2-microglobulin (beta 2m) reacting in ELISA with polyclonal and monoclonal human IgM rheumatoid factors (RF) as well as with monoclonal mouse IgG anti-beta 2m antibodies were studied after site-specific mutation of single or double beta 2m amino acid residues. Single site-specific mutations at lysine 58 and serine 61 produced a major decrease (50-100%) in reactivity of polyclonal IgM RF with beta 2m. Mutations at serine 57, tryptophane 60, and phenylalanine 62 also induced substantial decrements (25-49%) in IgM RF reactivity. beta 2m mutants containing double amino acid mutations including one residue outside the SKDWSFY region along with four different mutations at tryptophane 60 also often showed marked decrements in IgM RF anti-beta 2m reactivity. Site-specific mutations at virtually all residues within the SKDWSFY beta 2m region produced a major decrease in reactivity of two of three monoclonal human IgM RF. Results with nine murine IgG anti-beta 2m mAbs often showed an entirely different profile. Site-specific mutation of aspartic acid at position 59 produced a 50-100% decrease in binding of nine mAbs. Serine at position 61 and tyrosine at 63 also appeared to represent important residues for antigenic determinants reacting with anti-beta 2m mAbs. Results of mapping discrete epitopes using glycine substitution within overlapping 7-mers of beta 2m linear sequence compared with site-specific mutation of single beta 2m residues were similar in many instances, but also often showed marked differences. A marked change in antigenic contribution of single amino acid residues to beta 2m antigenic epitopes frequently depended on what residues were mutated to. Our findings emphasize that single residues within a small seven amino acid, solvent-accessible antigenic stretch of primary beta 2m sequence vary considerably in their contribution to the reactive antigenic structures for IgM RF as well as monoclonal IgG antibodies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>van Eyndhoven</LastName><ForeName>W G</ForeName><Initials>WG</Initials><AffiliationInfo><Affiliation>Department of Medicine, University of Florida, Gainesville 32610.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Malone</LastName><ForeName>C C</ForeName><Initials>CC</Initials></Author><Author ValidYN="Y"><LastName>Williams</LastName><ForeName>R C</ForeName><Initials>RC</Initials><Suffix>Jr</Suffix></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>AR1382421A2</GrantID><Acronym>AR</Acronym><Agency>NIAMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AR40438</GrantID><Acronym>AR</Acronym><Agency>NIAMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Clin Immunol Immunopathol</MedlineTA><NlmUniqueID>0356637</NlmUniqueID><ISSNLinking>0090-1229</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007074">Immunoglobulin G</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007075">Immunoglobulin 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MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004797" MajorTopicYN="N">Enzyme-Linked Immunosorbent Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007074" MajorTopicYN="N">Immunoglobulin G</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007075" MajorTopicYN="N">Immunoglobulin M</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012217" MajorTopicYN="N">Rheumatoid Factor</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001613" MajorTopicYN="N">beta 2-Microglobulin</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>9</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>3</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8062449</ArticleId><ArticleId IdType="pii">S0090122984711548</ArticleId><ArticleId IdType="doi">10.1006/clin.1994.1154</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Malone, C C" sort="Malone, C C" uniqKey="Malone C" first="C C" last="Malone">C C Malone</name><name sortKey="Van Eyndhoven, W G" sort="Van Eyndhoven, W G" uniqKey="Van Eyndhoven W" first="W G" last="Van Eyndhoven">W G Van Eyndhoven</name><name sortKey="Williams, R C" sort="Williams, R C" uniqKey="Williams R" first="R C" last="Williams">R C Williams</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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