Biophysical mechanism of the scavenger site near T cell-presented epitopes
We seek to identify consensus sequences in digested fragments of antigenic proteins regulating selection and major histocompatibility complex (MHC)-restricted presentation to T cells of epitopes within those fragments. One such pattern, of recurrent, hydrophobic sidechains forming a longitudinal hyd...
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| Veröffentlicht in: | Vaccine 1992, Vol.10 (1), p.3-7 |
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| container_title | Vaccine |
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| creator | Lu, S. Reyes, V.E. Bositis, C.M. Goldschmidt, T.G. Lam, V. Torgerson, R.R. Ciardelli, T. Hardy, L. Lew, R.A. Humphreys, R.E. |
| description | We seek to identify consensus sequences in digested fragments of antigenic proteins regulating selection and major histocompatibility complex (MHC)-restricted presentation to T cells of epitopes within those fragments. One such pattern, of recurrent, hydrophobic sidechains forming a longitudinal hydrophobic strip when a sequence is coiled as an α-helix, is found in or near most T cell-presented epitopes. Such recurrent hydrophobicity may lead to protease-protected coiling of the fragment against endosomal membranes and transfer to MHC molecules. This concept leads to better identification of T cell-presented sequences and possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction. |
| doi_str_mv | 10.1016/0264-410X(92)90410-L |
| format | Article |
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One such pattern, of recurrent, hydrophobic sidechains forming a longitudinal hydrophobic strip when a sequence is coiled as an α-helix, is found in or near most T cell-presented epitopes. Such recurrent hydrophobicity may lead to protease-protected coiling of the fragment against endosomal membranes and transfer to MHC molecules. This concept leads to better identification of T cell-presented sequences and possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction.</description><identifier>ISSN: 0264-410X</identifier><identifier>EISSN: 1873-2518</identifier><identifier>DOI: 10.1016/0264-410X(92)90410-L</identifier><identifier>PMID: 1371632</identifier><identifier>CODEN: VACCDE</identifier><language>eng</language><publisher>OXFORD: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Antigen processing ; Antigens ; Biological and medical sciences ; Chemical Phenomena ; Chemistry, Physical ; Epitopes - chemistry ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Histocompatibility antigens (hla, h-2 and other systems) ; Humans ; Immunology ; Life Sciences & Biomedicine ; Major Histocompatibility Complex - immunology ; Medicine, Research & Experimental ; MHC molecules ; Molecular immunology ; Molecular Sequence Data ; peptide vaccines ; Protein Conformation ; Research & Experimental Medicine ; Science & Technology ; T cell-presented epitope ; T-Lymphocytes - immunology ; α-helix</subject><ispartof>Vaccine, 1992, Vol.10 (1), p.3-7</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>9</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wosA1992HL74200001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c386t-24fa4f7b517c52409d0998c2f9ca86ca8e8bd964f4c90ec49064e9dab77048eb3</citedby><cites>FETCH-LOGICAL-c386t-24fa4f7b517c52409d0998c2f9ca86ca8e8bd964f4c90ec49064e9dab77048eb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0264-410X(92)90410-L$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,315,781,785,793,3551,4025,4055,27197,27927,27928,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5179674$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1371632$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lu, S.</creatorcontrib><creatorcontrib>Reyes, V.E.</creatorcontrib><creatorcontrib>Bositis, C.M.</creatorcontrib><creatorcontrib>Goldschmidt, T.G.</creatorcontrib><creatorcontrib>Lam, V.</creatorcontrib><creatorcontrib>Torgerson, R.R.</creatorcontrib><creatorcontrib>Ciardelli, T.</creatorcontrib><creatorcontrib>Hardy, L.</creatorcontrib><creatorcontrib>Lew, R.A.</creatorcontrib><creatorcontrib>Humphreys, R.E.</creatorcontrib><title>Biophysical mechanism of the scavenger site near T cell-presented epitopes</title><title>Vaccine</title><addtitle>VACCINE</addtitle><addtitle>Vaccine</addtitle><description>We seek to identify consensus sequences in digested fragments of antigenic proteins regulating selection and major histocompatibility complex (MHC)-restricted presentation to T cells of epitopes within those fragments. One such pattern, of recurrent, hydrophobic sidechains forming a longitudinal hydrophobic strip when a sequence is coiled as an α-helix, is found in or near most T cell-presented epitopes. Such recurrent hydrophobicity may lead to protease-protected coiling of the fragment against endosomal membranes and transfer to MHC molecules. This concept leads to better identification of T cell-presented sequences and possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigen processing</subject><subject>Antigens</subject><subject>Biological and medical sciences</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>Epitopes - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Histocompatibility antigens (hla, h-2 and other systems)</subject><subject>Humans</subject><subject>Immunology</subject><subject>Life Sciences & Biomedicine</subject><subject>Major Histocompatibility Complex - immunology</subject><subject>Medicine, Research & Experimental</subject><subject>MHC molecules</subject><subject>Molecular immunology</subject><subject>Molecular Sequence Data</subject><subject>peptide vaccines</subject><subject>Protein Conformation</subject><subject>Research & Experimental Medicine</subject><subject>Science & Technology</subject><subject>T cell-presented epitope</subject><subject>T-Lymphocytes - immunology</subject><subject>α-helix</subject><issn>0264-410X</issn><issn>1873-2518</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EZCTM</sourceid><sourceid>EIF</sourceid><recordid>eNqNkU1rFTEUhoMo9bb6DxSyEFFkNMlkPrIR6sXayoCbCu5CJnPijcwk0yS30n_fjHO53UkXIYHzvCc5TxB6RclHSmj9ibCaF5ySX-8Eey9IPhXdE7ShbVMWrKLtU7Q5Is_RaYx_CCFVScUJOqFlQ-uSbdD3L9bPu7totRrxBHqnnI0T9ganHeCo1S243xBwtAmwAxXwNdYwjsUcIIJLMGCYbfIzxBfomVFjhJeH_Qz9vPh6vb0suh_frrbnXaHLtk4F40Zx0_QVbXTFOBEDEaLVzAit2jovaPtB1NxwLQhoLkjNQQyqbxrCW-jLM_R27TsHf7OHmORk4_Im5cDvo2xYy6qy4hnkK6iDjzGAkXOwkwp3khK5KJSLH7n4kYLJfwpll2OvD_33_QTDQ2h1lutvDnWV_YwmKKdtPGJ5LlE3y-0fVuwv9N5EbcFpOFLnVAh22TWc5U8hNNPt4-mtTSpZ77Z-71KOfl6jkKXfWgjyEB9sAJ3k4O3_B74HByKudQ</recordid><startdate>1992</startdate><enddate>1992</enddate><creator>Lu, S.</creator><creator>Reyes, V.E.</creator><creator>Bositis, C.M.</creator><creator>Goldschmidt, T.G.</creator><creator>Lam, V.</creator><creator>Torgerson, R.R.</creator><creator>Ciardelli, T.</creator><creator>Hardy, L.</creator><creator>Lew, R.A.</creator><creator>Humphreys, R.E.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>BLEPL</scope><scope>DTL</scope><scope>EZCTM</scope><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></search><sort><creationdate>1992</creationdate><title>Biophysical mechanism of the scavenger site near T cell-presented epitopes</title><author>Lu, S. ; Reyes, V.E. ; Bositis, C.M. ; Goldschmidt, T.G. ; Lam, V. ; Torgerson, R.R. ; Ciardelli, T. ; Hardy, L. ; Lew, R.A. ; Humphreys, R.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-24fa4f7b517c52409d0998c2f9ca86ca8e8bd964f4c90ec49064e9dab77048eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigen processing</topic><topic>Antigens</topic><topic>Biological and medical sciences</topic><topic>Chemical Phenomena</topic><topic>Chemistry, Physical</topic><topic>Epitopes - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Histocompatibility antigens (hla, h-2 and other systems)</topic><topic>Humans</topic><topic>Immunology</topic><topic>Life Sciences & Biomedicine</topic><topic>Major Histocompatibility Complex - immunology</topic><topic>Medicine, Research & Experimental</topic><topic>MHC molecules</topic><topic>Molecular immunology</topic><topic>Molecular Sequence Data</topic><topic>peptide vaccines</topic><topic>Protein Conformation</topic><topic>Research & Experimental Medicine</topic><topic>Science & Technology</topic><topic>T cell-presented epitope</topic><topic>T-Lymphocytes - immunology</topic><topic>α-helix</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lu, S.</creatorcontrib><creatorcontrib>Reyes, V.E.</creatorcontrib><creatorcontrib>Bositis, C.M.</creatorcontrib><creatorcontrib>Goldschmidt, T.G.</creatorcontrib><creatorcontrib>Lam, V.</creatorcontrib><creatorcontrib>Torgerson, R.R.</creatorcontrib><creatorcontrib>Ciardelli, T.</creatorcontrib><creatorcontrib>Hardy, L.</creatorcontrib><creatorcontrib>Lew, R.A.</creatorcontrib><creatorcontrib>Humphreys, R.E.</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 1992</collection><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><jtitle>Vaccine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lu, S.</au><au>Reyes, V.E.</au><au>Bositis, C.M.</au><au>Goldschmidt, T.G.</au><au>Lam, V.</au><au>Torgerson, R.R.</au><au>Ciardelli, T.</au><au>Hardy, L.</au><au>Lew, R.A.</au><au>Humphreys, R.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biophysical mechanism of the scavenger site near T cell-presented epitopes</atitle><jtitle>Vaccine</jtitle><stitle>VACCINE</stitle><addtitle>Vaccine</addtitle><date>1992</date><risdate>1992</risdate><volume>10</volume><issue>1</issue><spage>3</spage><epage>7</epage><pages>3-7</pages><issn>0264-410X</issn><eissn>1873-2518</eissn><coden>VACCDE</coden><abstract>We seek to identify consensus sequences in digested fragments of antigenic proteins regulating selection and major histocompatibility complex (MHC)-restricted presentation to T cells of epitopes within those fragments. One such pattern, of recurrent, hydrophobic sidechains forming a longitudinal hydrophobic strip when a sequence is coiled as an α-helix, is found in or near most T cell-presented epitopes. Such recurrent hydrophobicity may lead to protease-protected coiling of the fragment against endosomal membranes and transfer to MHC molecules. This concept leads to better identification of T cell-presented sequences and possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction.</abstract><cop>OXFORD</cop><pub>Elsevier Ltd</pub><pmid>1371632</pmid><doi>10.1016/0264-410X(92)90410-L</doi><tpages>5</tpages></addata></record> |
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| source | Web of Science - Science Citation Index Expanded - 1992<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Animals Antigen processing Antigens Biological and medical sciences Chemical Phenomena Chemistry, Physical Epitopes - chemistry Fundamental and applied biological sciences. Psychology Fundamental immunology Histocompatibility antigens (hla, h-2 and other systems) Humans Immunology Life Sciences & Biomedicine Major Histocompatibility Complex - immunology Medicine, Research & Experimental MHC molecules Molecular immunology Molecular Sequence Data peptide vaccines Protein Conformation Research & Experimental Medicine Science & Technology T cell-presented epitope T-Lymphocytes - immunology α-helix |
| title | Biophysical mechanism of the scavenger site near T cell-presented epitopes |
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