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Dear users, welcome to the new interface of the Charles University Publication Repository. We would appreciate it if you could take a moment of your time to provide us with feedback on the new design of the repository.
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Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores
dc.contributor.author | Lepesheva, Anna | |
dc.contributor.author | Grobarčíková, Michaela | |
dc.contributor.author | Osičková, Adriana | |
dc.contributor.author | Jurnečka, David | |
dc.contributor.author | Knoblochová, Šárka | |
dc.contributor.author | Čížková, Monika | |
dc.contributor.author | Osička, Radim | |
dc.contributor.author | Šebo, Peter | |
dc.contributor.author | Mašín, Jiří | |
dc.date.accessioned | 2024-06-17T11:15:37Z | |
dc.date.available | 2024-06-17T11:15:37Z | |
dc.date.issued | 2024 | |
dc.identifier.uri | https://hdl.handle.net/20.500.14178/2504 | |
dc.description.abstract | The acylated pore-forming Repeats in ToXin (RTX) cytolysins alpha-hemolysin (HlyA) and adenylate cyclase toxin (CyaA) preferentially bind to beta 2 integrins of myeloid leukocytes but can also promiscuously bind and permeabilize cells lacking the beta 2 integrins. We constructed a HlyA1-563/CyaA860-1706 chimera that was acylated either by the toxin-activating acyltransferase CyaC, using sixteen carbon-long (C16) acyls, or by the HlyC acyltransferase using fourteen carbon-long (C14) acyls. Cytolysin assays with the C16- or C14-acylated HlyA/ CyaA chimeric toxin revealed that the RTX domain of CyaA can functionally replace the RTX domain of HlyA only if it is modified by C16-acyls on the Lys983 residue of CyaA. The C16-monoacylated HlyA/CyaA chimera was as pore-forming and cytolytic as native HlyA, whereas the C14-acylated chimera exhibited very low poreforming activity. Hence, the capacity of the RTX domain of CyaA to support the insertion of the N-terminal pore-forming domain into the target cell membrane, and promote formation of toxin pores, strictly depends on the modification of the Lys983 residue by an acyl chain of adapted length. | en |
dc.language.iso | en | |
dc.relation.url | https://doi.org/10.1016/j.bbamem.2024.184311 | |
dc.rights | Creative Commons Uveďte původ 4.0 International | cs |
dc.rights | Creative Commons Attribution 4.0 International | en |
dc.title | Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores | en |
dcterms.accessRights | openAccess | |
dcterms.license | https://creativecommons.org/licenses/by/4.0/legalcode | |
dc.date.updated | 2024-06-17T11:15:37Z | |
dc.subject.keyword | RTX toxin | en |
dc.subject.keyword | adenylate cyclase toxin | en |
dc.subject.keyword | alpha-hemolysin | en |
dc.subject.keyword | chimera | en |
dc.subject.keyword | fatty acylation | en |
dc.subject.keyword | cytotoxicity | en |
dc.identifier.eissn | 1879-2642 | |
dc.relation.fundingReference | info:eu-repo/grantAgreement/UK/COOP/COOP | |
dc.relation.fundingReference | info:eu-repo/grantAgreement/MSM//LX22NPO5103 | |
dc.date.embargoStartDate | 2024-06-17 | |
dc.type.obd | 73 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | |
dc.identifier.doi | 10.1016/j.bbamem.2024.184311 | |
dc.identifier.utWos | 001227325000001 | |
dc.identifier.eidScopus | 2-s2.0-85189966925 | |
dc.identifier.obd | 648496 | |
dc.identifier.pubmed | 38570122 | |
dc.subject.rivPrimary | 10000::10600::10606 | |
dc.relation.datasetUrl | https://www.ebi.ac.uk/pride/archive/projects/PXD046160 | |
dcterms.isPartOf.name | Biochimica et Biophysica Acta - Biomembranes | |
dcterms.isPartOf.issn | 0005-2736 | |
dcterms.isPartOf.journalYear | 2024 | |
dcterms.isPartOf.journalVolume | 1866 | |
dcterms.isPartOf.journalIssue | 5 | |
uk.faculty.primaryId | 115 | |
uk.faculty.primaryName | Přírodovědecká fakulta | cs |
uk.faculty.primaryName | Faculty of Science | en |
uk.department.primaryId | 1034 | |
uk.department.primaryName | Katedra genetiky a mikrobiologie | cs |
uk.department.primaryName | Department of Genetics and Microbiology | en |
dc.type.obdHierarchyCs | ČLÁNEK V ČASOPISU::článek v časopisu::původní článek | cs |
dc.type.obdHierarchyEn | JOURNAL ARTICLE::journal article::original article | en |
dc.type.obdHierarchyCode | 73::152::206 | en |
uk.displayTitle | Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores | en |