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The proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complex

dc.contributor.authorSEEFELDT, A. Carolin
dc.contributor.authorFABIAN, Nguyen
dc.contributor.authorANTUNES, Stephanie
dc.contributor.authorPEREBASKINE, Natacha
dc.contributor.authorGRAF, Michael
dc.contributor.authorARENZ, Stefan
dc.contributor.authorINAMPUDI, K. Kishore
dc.contributor.authorDOUAT, Celine
dc.contributor.authorGUICHARD, Gilles
dc.contributor.authorWILSON, Daniel N.
dc.contributor.authorINNIS, C. Axel
dc.date.accessioned2020-09-03T08:01:54Z
dc.date.available2020-09-03T08:01:54Z
dc.date.issued2015
dc.identifier.issn1545-9993
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10923
dc.description.abstractEnThe increasing prevalence of multidrug-resistant pathogenic bacteria is making current antibiotics obsolete. Proline-rich antimicrobial peptides (PrAMPs) display potent activity against Gram-negative bacteria and thus represent an avenue for antibiotic development. PrAMPs from the oncocin family interact with the ribosome to inhibit translation, but their mode of action has remained unclear. Here we have determined a structure of the Onc112 peptide in complex with the Thermus thermophilus 70S ribosome at a resolution of 3.1 angstrom by X-ray crystallography. The Onc112 peptide binds within the ribosomal exit tunnel and extends toward the peptidyl transferase center, where it overlaps with the binding site for an aminoacyl-tRNA. We show biochemically that the binding of Onc112 blocks and destabilizes the initiation complex, thus preventing entry into the elongation phase. Our findings provide a basis for the future development of this class of potent antimicrobial agents.
dc.language.isoen
dc.title.enThe proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complex
dc.typeArticle de revue
dc.identifier.doi10.1038/nsmb.3034
dc.subject.halChimie/Matériaux
bordeaux.journalNature Structural & Molecular Biology
bordeaux.page470-U59
bordeaux.volume22
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue6
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nature%20Structural%20&%20Molecular%20Biology&rft.date=2015&rft.volume=22&rft.issue=6&rft.spage=470-U59&rft.epage=470-U59&rft.eissn=1545-9993&rft.issn=1545-9993&rft.au=SEEFELDT,%20A.%20Carolin&FABIAN,%20Nguyen&ANTUNES,%20Stephanie&PEREBASKINE,%20Natacha&GRAF,%20Michael&rft.genre=article


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