A novel recognition motif of human NKT antigen receptor for a glycolipid ligand
Murine NKT cells can recognize α-galactosylceramide (α-GalCer) in the context of a class Ib CD1d molecule. Here we show that α-GalCer can selectively activate freshly isolated human Vα24+Vβ11+ cells, functionally defining the human NKT cells. The naive human NKT cell repertoire consisted of cells ex...
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Veröffentlicht in: | International immunology 1999-06, Vol.11 (6), p.881-887 |
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creator | Kawano, Tetsu Tanaka, Yujiro Shimizu, Eiko Kaneko, Yoshikatsu Kamata, Noriaki Sato, Hiroshi Osada, Hisao Sekiya, Soei Nakayama, Toshinori Taniguchi, Masaru |
description | Murine NKT cells can recognize α-galactosylceramide (α-GalCer) in the context of a class Ib CD1d molecule. Here we show that α-GalCer can selectively activate freshly isolated human Vα24+Vβ11+ cells, functionally defining the human NKT cells. The naive human NKT cell repertoire consisted of cells expressing an invariant Vα24JαQ chain and a diverse array of β chains derived from a single Vβ11 gene segment. Stimulation with α-GalCer expanded a polyclonal subset of the human NKT cell repertoire carrying a novel complementarity-determining region (CDR) 3β consensus motif that may directly interact with the sugar moiety of α-GalCer. Our data suggest that certain redundancy is allowed for CDR3β of NKT antigen receptor to interact with the ligand and provide a first clue to understand the novel protein–carbohydrate interaction mechanisms. |
doi_str_mv | 10.1093/intimm/11.6.881 |
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Here we show that α-GalCer can selectively activate freshly isolated human Vα24+Vβ11+ cells, functionally defining the human NKT cells. The naive human NKT cell repertoire consisted of cells expressing an invariant Vα24JαQ chain and a diverse array of β chains derived from a single Vβ11 gene segment. Stimulation with α-GalCer expanded a polyclonal subset of the human NKT cell repertoire carrying a novel complementarity-determining region (CDR) 3β consensus motif that may directly interact with the sugar moiety of α-GalCer. Our data suggest that certain redundancy is allowed for CDR3β of NKT antigen receptor to interact with the ligand and provide a first clue to understand the novel protein–carbohydrate interaction mechanisms.</description><identifier>ISSN: 0953-8178</identifier><identifier>ISSN: 1460-2377</identifier><identifier>EISSN: 1460-2377</identifier><identifier>DOI: 10.1093/intimm/11.6.881</identifier><identifier>PMID: 10360961</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Adult ; Animals ; Antigens, CD1 - immunology ; Antigens, CD1d ; APC antigen-presenting cell ; Binding Sites - immunology ; carbohydrate-binding proteins ; CDR3 complementarity-determining region 3 ; complementarity-determining region ; CRD carbohydrate-recognition domain ; Fetal Blood - cytology ; Fetal Blood - immunology ; Galactosylceramides - immunology ; Galactosylceramides - metabolism ; Humans ; Killer Cells, Natural - immunology ; Killer Cells, Natural - metabolism ; Ligands ; Lymphocyte Activation - immunology ; Mice ; NKT antigen receptor ; PE phycoerythrin ; protein–sugar interaction ; Receptors, Antigen, T-Cell, alpha-beta - immunology ; Receptors, Antigen, T-Cell, alpha-beta - metabolism ; repertoire selection ; T-Lymphocyte Subsets - immunology ; α-GalCer α-galactosylceramide</subject><ispartof>International immunology, 1999-06, Vol.11 (6), p.881-887</ispartof><rights>Copyright Oxford University Press Jun 1999</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c459t-79d168730f4851826d80ff05cb117ea71a0397d4d679100d2a2ef37c7ce71c033</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10360961$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kawano, Tetsu</creatorcontrib><creatorcontrib>Tanaka, Yujiro</creatorcontrib><creatorcontrib>Shimizu, Eiko</creatorcontrib><creatorcontrib>Kaneko, Yoshikatsu</creatorcontrib><creatorcontrib>Kamata, Noriaki</creatorcontrib><creatorcontrib>Sato, Hiroshi</creatorcontrib><creatorcontrib>Osada, Hisao</creatorcontrib><creatorcontrib>Sekiya, Soei</creatorcontrib><creatorcontrib>Nakayama, Toshinori</creatorcontrib><creatorcontrib>Taniguchi, Masaru</creatorcontrib><title>A novel recognition motif of human NKT antigen receptor for a glycolipid ligand</title><title>International immunology</title><addtitle>Int. Immunol</addtitle><description>Murine NKT cells can recognize α-galactosylceramide (α-GalCer) in the context of a class Ib CD1d molecule. Here we show that α-GalCer can selectively activate freshly isolated human Vα24+Vβ11+ cells, functionally defining the human NKT cells. The naive human NKT cell repertoire consisted of cells expressing an invariant Vα24JαQ chain and a diverse array of β chains derived from a single Vβ11 gene segment. Stimulation with α-GalCer expanded a polyclonal subset of the human NKT cell repertoire carrying a novel complementarity-determining region (CDR) 3β consensus motif that may directly interact with the sugar moiety of α-GalCer. 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Our data suggest that certain redundancy is allowed for CDR3β of NKT antigen receptor to interact with the ligand and provide a first clue to understand the novel protein–carbohydrate interaction mechanisms.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>10360961</pmid><doi>10.1093/intimm/11.6.881</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
subjects | Adult Animals Antigens, CD1 - immunology Antigens, CD1d APC antigen-presenting cell Binding Sites - immunology carbohydrate-binding proteins CDR3 complementarity-determining region 3 complementarity-determining region CRD carbohydrate-recognition domain Fetal Blood - cytology Fetal Blood - immunology Galactosylceramides - immunology Galactosylceramides - metabolism Humans Killer Cells, Natural - immunology Killer Cells, Natural - metabolism Ligands Lymphocyte Activation - immunology Mice NKT antigen receptor PE phycoerythrin protein–sugar interaction Receptors, Antigen, T-Cell, alpha-beta - immunology Receptors, Antigen, T-Cell, alpha-beta - metabolism repertoire selection T-Lymphocyte Subsets - immunology α-GalCer α-galactosylceramide |
title | A novel recognition motif of human NKT antigen receptor for a glycolipid ligand |
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