Acylation of the Bordetella pertussis CyaA-hemolysin: Functional implications for efficient membrane insertion and pore formation

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• 作者：Kanungsuk Meetum^a ; Chompounoot Imtong^b ; Gerd Katzenmeier^a ; Chanan Angsuthanasombat^a ; ^c ; ^{chanan.ang@mahidol.ac.th}
• 关键词：CyaA-Hly ; CyaA-hemolysin ; Ch ; cholesterol ; DiPhyPC ; 1 ; 2-diphytanoyl-sn-glycero-3-phosphocholine ; DOPC ; 1 ; 2-dioleoyl-sn-glycerol-3-phosphocholine ; DOPE ; 1 ; 2-dioleoyl-sn-glycerol-3-phosphoethanolamine ; NA/CyaA-Hly ; non-acylated CyaA-Hly ; Ni2  ; +-NTA ; nickel-nitrilotriacetic acid ; PLBs ; planar lipid bilayers ; RTX ; Repeat-in-ToXin
• 刊名：Biochimica et Biophysica Acta (BBA) - Biomembranes
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1859
• 期：3
• 页码：312-318
• 全文大小：1027 K
• 卷排序：1859

文摘

CyaA-hemolysin domain (CyaA-Hly)-induced hemolysis is activated via palmitoylation at Lys983. No severe conformational change occurs upon acylation at Lys983 of CyaA-Hly. Acylation is not required for either toxin binding to target membranes or channel conductivity. Lys983-linked palmitoyl is required for stabilizing CyaA-Hly-induced channels.