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Synthesis of Multivalent Glycoconjugates Containing the Immunoactive LELTE Peptide: Effect of Glycosylation on Cellular Activation and Natural Killing by Human Peripheral Blood Mononuclear Cells

  1. 1.
    SYSNO ASEP0348154
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleSynthesis of Multivalent Glycoconjugates Containing the Immunoactive LELTE Peptide: Effect of Glycosylation on Cellular Activation and Natural Killing by Human Peripheral Blood Mononuclear Cells
    Author(s) Renaudet, O. (FR)
    Křenek, Karel (MBU-M)
    Bossu, I. (FR)
    Dumy, P. (FR)
    Kádek, A. (CZ)
    Adámek, David (MBU-M)
    Vaněk, O. (CZ)
    Kavan, Daniel (MBU-M) RID, ORCID
    Gažák, Radek (MBU-M) RID, ORCID
    Šulc, Miroslav (MBU-M) RID, ORCID
    Bezouška, K. (CZ)
    Křen, Vladimír (MBU-M) RID, ORCID
    Source TitleJournal of the American Chemical Society. - : American Chemical Society - ISSN 0002-7863
    Roč. 132, č. 19 (2010), s. 6800-6808
    Number of pages9 s.
    Languageeng - English
    CountryUS - United States
    KeywordsKILLER-CELLS ; TN ANTIGEN ; RECEPTOR
    Subject RIVEE - Microbiology, Virology
    R&D ProjectsLC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    1M0505 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    IAA400200503 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    GA303/09/0477 GA ČR - Czech Science Foundation (CSF)
    GD305/09/H008 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z50200510 - MBU-M (2005-2011)
    UT WOS000277721500040
    DOI10.1021/ja101296t
    AnnotationPentapeptide diacidic sequence LELTE, derived from the mycobacterial heat shock protein hsp65, has been recently identified as a “danger” signal of the immune system effective via specific binding to the universal leukocyte triggering receptor CD69. This sequence is not active per se, only after its presentation within the multivalent environment of its parent protein, or after artificial dimerization using a standard bifunctional reagents. Here we describe an entirely new way of presenting of this peptide based on its attachment to a cyclopeptide RAFT scaffold (K-K-K-P-G)2 through the ε-amino group of lysine residues, alone or in combination with the carbohydrate epitope αGalNAc. The ability of such RAFT scaffolds to precipitate the target CD69 receptor or to activate CD69-positive cells is enhanced in compounds 2 and 4 possessing combined peptide/carbohydrate expression. Compounds 2 and 4 are highly efficient activators of natural killer lymphocytes
    WorkplaceInstitute of Microbiology
    ContactEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Year of Publishing2011
Number of the records: 1  

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