The Role of D-Alanine in the Antigenic Specificity of Bacterial Mucopeptides
Mucopeptides extracted from Gram-positive cocci reacted with antisera against the synthetic random polypeptides poly (l-glu42-l-lys28-d-ala30)n and poly (d-glu16-l-lys16-dl-ala68)n. Quantitative precipitin inhibition studies employing a haptenic inhibitor derived from bacterial mucopeptide and synth...
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Veröffentlicht in: | The Journal of immunology (1950) 1970-01, Vol.104 (1), p.230-237 |
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creator | Karakawa, Walter W Maurer, Paul H Walsh, Patricia Krause, Richard M |
description | Mucopeptides extracted from Gram-positive cocci reacted with antisera against the synthetic random polypeptides poly (l-glu42-l-lys28-d-ala30)n and poly (d-glu16-l-lys16-dl-ala68)n. Quantitative precipitin inhibition studies employing a haptenic inhibitor derived from bacterial mucopeptide and synthetic peptides and polypeptides indicated that d-alanine is a critical amino acid in the antigenic determinant responsible for the cross-reactivity. Only copolymers containing d-alanine residues were effective inhibitors of the cross-reactivity.
The results of passive hemagglutination studies of appropriately coated erythrocytes and mucopeptide agglutination reactions with antimucopeptide sera and anti-synthetic polypeptide sera indicated that the immunologic relationship between bacterial mucopeptide and the synthetic copolymers of amino acids is predominantly associated with the presence of d-alanine in the determinant grouping. |
doi_str_mv | 10.4049/jimmunol.104.1.230 |
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The results of passive hemagglutination studies of appropriately coated erythrocytes and mucopeptide agglutination reactions with antimucopeptide sera and anti-synthetic polypeptide sera indicated that the immunologic relationship between bacterial mucopeptide and the synthetic copolymers of amino acids is predominantly associated with the presence of d-alanine in the determinant grouping.</description><identifier>ISSN: 0022-1767</identifier><identifier>EISSN: 1550-6606</identifier><identifier>DOI: 10.4049/jimmunol.104.1.230</identifier><identifier>PMID: 5411504</identifier><language>eng</language><publisher>United States: Am Assoc Immnol</publisher><subject>Alanine ; Animals ; Antigen-Antibody Reactions ; Antigens ; Bacterial Proteins ; Cell Wall - immunology ; Cross Reactions ; Erythrocytes - immunology ; Hemagglutination Inhibition Tests ; Hemagglutination Tests ; Immune Sera ; Mucoproteins ; Peptides - chemical synthesis ; Polymers - chemical synthesis ; Precipitin Tests ; Rabbits ; Streptococcus - immunology</subject><ispartof>The Journal of immunology (1950), 1970-01, Vol.104 (1), p.230-237</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-8a761d61131c61dd7c064ab6c407f57c0c9c465f76873b5c60fb74289abec8db3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5411504$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Karakawa, Walter W</creatorcontrib><creatorcontrib>Maurer, Paul H</creatorcontrib><creatorcontrib>Walsh, Patricia</creatorcontrib><creatorcontrib>Krause, Richard M</creatorcontrib><title>The Role of D-Alanine in the Antigenic Specificity of Bacterial Mucopeptides</title><title>The Journal of immunology (1950)</title><addtitle>J Immunol</addtitle><description>Mucopeptides extracted from Gram-positive cocci reacted with antisera against the synthetic random polypeptides poly (l-glu42-l-lys28-d-ala30)n and poly (d-glu16-l-lys16-dl-ala68)n. Quantitative precipitin inhibition studies employing a haptenic inhibitor derived from bacterial mucopeptide and synthetic peptides and polypeptides indicated that d-alanine is a critical amino acid in the antigenic determinant responsible for the cross-reactivity. Only copolymers containing d-alanine residues were effective inhibitors of the cross-reactivity.
The results of passive hemagglutination studies of appropriately coated erythrocytes and mucopeptide agglutination reactions with antimucopeptide sera and anti-synthetic polypeptide sera indicated that the immunologic relationship between bacterial mucopeptide and the synthetic copolymers of amino acids is predominantly associated with the presence of d-alanine in the determinant grouping.</description><subject>Alanine</subject><subject>Animals</subject><subject>Antigen-Antibody Reactions</subject><subject>Antigens</subject><subject>Bacterial Proteins</subject><subject>Cell Wall - immunology</subject><subject>Cross Reactions</subject><subject>Erythrocytes - immunology</subject><subject>Hemagglutination Inhibition Tests</subject><subject>Hemagglutination Tests</subject><subject>Immune Sera</subject><subject>Mucoproteins</subject><subject>Peptides - chemical synthesis</subject><subject>Polymers - chemical synthesis</subject><subject>Precipitin Tests</subject><subject>Rabbits</subject><subject>Streptococcus - immunology</subject><issn>0022-1767</issn><issn>1550-6606</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkMlOwzAQhi0EKqXwAkhIOXFLGCdekmMpq1SEBOVsOY7TunIW4kRR3x5XLXCa7Z9_Rh9C1xgiAiS725qqGurGRhhIhKM4gRM0xZRCyBiwUzQFiOMQc8bP0YVzWwBgEJMJmlCCMQUyRcvVRgcfjdVBUwYP4dzK2tQ6MHXQ-8G87s1a10YFn61WpjTK9Lu98l6qXndG2uBtUE2r294U2l2is1Jap6-OcYa-nh5Xi5dw-f78upgvQ0WSrA9TyRkuGMYJVj4puAJGZM4UAV5SX6lMEUZLzlKe5FQxKHNO4jSTuVZpkSczdHvwbbvme9CuF5VxSlv_vG4GJ1JCOCQp9cL4IFRd41ynS9F2ppLdTmAQe4TiF6FvEIGFR-iXbo7uQ17p4m_lyOz_-sasN6PptHCVtNarsRjH8d_oByYpe1Q</recordid><startdate>19700101</startdate><enddate>19700101</enddate><creator>Karakawa, Walter W</creator><creator>Maurer, Paul H</creator><creator>Walsh, Patricia</creator><creator>Krause, Richard M</creator><general>Am Assoc Immnol</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>7X8</scope></search><sort><creationdate>19700101</creationdate><title>The Role of D-Alanine in the Antigenic Specificity of Bacterial Mucopeptides</title><author>Karakawa, Walter W ; Maurer, Paul H ; Walsh, Patricia ; Krause, Richard M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-8a761d61131c61dd7c064ab6c407f57c0c9c465f76873b5c60fb74289abec8db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Alanine</topic><topic>Animals</topic><topic>Antigen-Antibody Reactions</topic><topic>Antigens</topic><topic>Bacterial Proteins</topic><topic>Cell Wall - immunology</topic><topic>Cross Reactions</topic><topic>Erythrocytes - immunology</topic><topic>Hemagglutination Inhibition Tests</topic><topic>Hemagglutination Tests</topic><topic>Immune Sera</topic><topic>Mucoproteins</topic><topic>Peptides - chemical synthesis</topic><topic>Polymers - chemical synthesis</topic><topic>Precipitin Tests</topic><topic>Rabbits</topic><topic>Streptococcus - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karakawa, Walter W</creatorcontrib><creatorcontrib>Maurer, Paul H</creatorcontrib><creatorcontrib>Walsh, Patricia</creatorcontrib><creatorcontrib>Krause, Richard M</creatorcontrib><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><jtitle>The Journal of immunology (1950)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Karakawa, Walter W</au><au>Maurer, Paul H</au><au>Walsh, Patricia</au><au>Krause, Richard M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Role of D-Alanine in the Antigenic Specificity of Bacterial Mucopeptides</atitle><jtitle>The Journal of immunology (1950)</jtitle><addtitle>J Immunol</addtitle><date>1970-01-01</date><risdate>1970</risdate><volume>104</volume><issue>1</issue><spage>230</spage><epage>237</epage><pages>230-237</pages><issn>0022-1767</issn><eissn>1550-6606</eissn><abstract>Mucopeptides extracted from Gram-positive cocci reacted with antisera against the synthetic random polypeptides poly (l-glu42-l-lys28-d-ala30)n and poly (d-glu16-l-lys16-dl-ala68)n. Quantitative precipitin inhibition studies employing a haptenic inhibitor derived from bacterial mucopeptide and synthetic peptides and polypeptides indicated that d-alanine is a critical amino acid in the antigenic determinant responsible for the cross-reactivity. Only copolymers containing d-alanine residues were effective inhibitors of the cross-reactivity.
The results of passive hemagglutination studies of appropriately coated erythrocytes and mucopeptide agglutination reactions with antimucopeptide sera and anti-synthetic polypeptide sera indicated that the immunologic relationship between bacterial mucopeptide and the synthetic copolymers of amino acids is predominantly associated with the presence of d-alanine in the determinant grouping.</abstract><cop>United States</cop><pub>Am Assoc Immnol</pub><pmid>5411504</pmid><doi>10.4049/jimmunol.104.1.230</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Alanine Animals Antigen-Antibody Reactions Antigens Bacterial Proteins Cell Wall - immunology Cross Reactions Erythrocytes - immunology Hemagglutination Inhibition Tests Hemagglutination Tests Immune Sera Mucoproteins Peptides - chemical synthesis Polymers - chemical synthesis Precipitin Tests Rabbits Streptococcus - immunology |
title | The Role of D-Alanine in the Antigenic Specificity of Bacterial Mucopeptides |
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