Isolated CyaA-RTX subdomain from Bordetella pertussis: Structural and functional implications for its interaction with target erythrocyte membranes
详细信息 查看全文
- 作者：Riyaz Ahmad Pandita ; Kanungsuk Meetumb ; Kittipong Suvarnapunyaa ; Gerd Katzenmeierb ; Wanpen Chaicumpac ; Chanan Angsuthanasombatb ; d ; chanan.ang@mahidol.ac.th" class="auth_mail" title="E-mail the corresponding author
- 关键词：Bordetella pertussis ; CyaA-hemolysin ; CyaA-RTX ; Erythrocyte-membrane interaction ; WW domain family
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2015
- 出版时间：9 October 2015
- 年：2015
- 卷：466
- 期：1
- 页码：76-81
- 全文大小：1371 K
文摘
- •
CyaA-RTX subdomain of CyaA-Hly was over-expressed in isolation as soluble, native-folded form.
- •
Isolated 100-kDa CyaA-RTX subdomain retains functionality for binding to target erythrocytes.
- •
Capability of CyaA-RTX to neutralize CyaA-Hly-induced hemolysis was diminished by anti-RTX antisera.
- •
3D-modeled CyaA-RTX revealed Linker II-loop structure sharing sequence similarity to human WW domains.
- •
CyaA-RTX Linker II represents a functional segment harboring a critical motif for receptor-binding activity.