Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores.

0585467 - MBÚ 2025 RIV NL eng J - Journal Article
Lepesheva, Anna - Grobarčíková, Michaela - Osičková, Adriana - Jurnečka, David - Knoblochová, Šárka - Čížková, Monika - Osička, Radim - Šebo, Peter - Mašín, Jiří
Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores.
Biochimica Et Biophysica Acta-Biomembranes. Roč. 1866, č. 5 (2024), s. 184311. ISSN 0005-2736. E-ISSN 1879-2642
R&D Projects: GA ČR(CZ) GA22-15825S; GA ČR(CZ) GA22-01558S; GA ČR(CZ) GX19-27630X; GA MŠMT(CZ) LX22NPO5103; GA MŠMT(CZ) EH22_008/0004597
Research Infrastructure: EATRIS-CZ IV - 90253; CIISB III - 90242
Institutional support: RVO:61388971
Keywords : RTX toxin * Adenylate cyclase toxin * α-Hemolysin * Chimera * Fatty acylation * Cytotoxicity
OECD category: Microbiology
Impact factor: 3.4, year: 2022
Method of publishing: Open access
https://www.sciencedirect.com/science/article/pii/S0005273624000427?via%3Dihub

We constructed an HlyA1–563/CyaA860–1706 chimera to test the hypothesis that the RTX domain and its acylated segment (residues
860 to 1706 of CyaA) may deliver into cell membrane and might thus support the formation of cytolytic pores by an N-terminally linked poreforming domain derived from HlyA. We show that this was the case only when the Lys983 residue of the RTX moiety of CyaA was acylated by a C16 acyl of adapted length, whereas a shorter C14 acyl conferred on the toxin chimera a much lower capacity to insert the HlyA-derived poreforming domain into cell membrane. This work reveals the requirement for a structural match between the attached acyl chain of adapted length and the structure of the acylated RTX domain cap.

Permanent Link: https://hdl.handle.net/11104/0353157


Research data: the ProteomeXchange Consortium via the PRIDE partner repository with the data set identifier PXD046160