The Streptococcus agalactiae Ribose Binding Protein B (RbsB) Mediates Quorum Sensing Signal Uptake via Interaction with Autoinducer-2 Signals

doi:10.1007/s11802-021-4810-4

IOCAS-IR > 实验海洋生物学重点实验室

	The Streptococcus agalactiae Ribose Binding Protein B (RbsB) Mediates Quorum Sensing Signal Uptake via Interaction with Autoinducer-2 Signals
	Fan Bolin 1; Pan Lixia 2; Wang Zhongliang 1; Eakapol, Wangkahart 5; Huang Yuchong 1,3,4; Yang Dengfeng 6; Jian Jichang 1,3,4; Huang Yu 1,3,4; Wang Bei1,3,4
	2021-10-01
发表期刊	JOURNAL OF OCEAN UNIVERSITY OF CHINA
ISSN	1672-5182
卷号	20 期号:5 页码:1285-1295
通讯作者	Wang Bei([email protected])
摘要	Understanding aquatic pathogen in sediments or aquacultural water is crucial to protect public health from soilborne and waterborne diseases. Quorum sensing (QS) was increasingly reported in biological wastewater treatment processes because of their inherent roles in biofilm development, bacterial aggregation and so on. The widely QS signals was Antoinducer-2 (AI-2), primarily involved to allow the possibility of interspecies communication. However, the cellular components that mediate the response of Streptococcus agalactiae to AI-2 have not been fully characterized. Analysis of the complete genome sequence of S. agalactiae indicated that its RbsB protein has similarity to Escherichia coli LsrB and Aggregatibacter actinomycetemcomitans RbsB proteins that bind AI-2. We hypothesized that RbsB protein mediates quorum sensing signal uptake via interaction with AI-2. To evaluate the regulatory effect of RbsB on QS system, the recombinant plasmid pGEX-6p-1-RbsB was constructed and RbsB protein was purified with GST-tag. To further elucidate the role of RbsB protein binding to DPD (AI-2 precursor dihydroxypentanedione), the systematically throughput circular dichroism (CD) spectroscopy, isothermal titration calorimetry(200) (ITC200) and molecular docking methods were employed. The high expression of soluble RbsB protein with molecular weight of 33 kDa was obtained. The thermodynamics results (Delta H <0, Delta S < 0, Delta G *lt; 0) with ITC determination indicated that the binding process between DPD and RbsB was exothermic and spontaneous, with hydrogen bonds and van der Waals forces as the main binding forces. Obviously, DPD can be more easily combined with RbsB in a dose-dependent manner, suggesting that RbsB was changed in the microenvironment of DPD when the DPD concentration was between 0.8-1.0 mmolL(-1) and reaching the maximum binding amount. According to molecular docking, 3 hydrophobic residues involved in DPD and RbsB protein stable binding were be found, and also hydrogen bonding plays a key role in the formation of the new complex. RbsB efficiently inhibited V. harveyi bioluminescence induced by both S. agalactiae AI-2 and V. harveyi AI-2 in a dose-dependent manner. However, our results suggest that RbsB may play a role in the response of S. agalactiace to AI-2.
关键词	Streptococcus agalactiae RbsB protein circular dichroism (CD) spectroscopy isothermal titration calorimetry(200) (ITC200) molecular docking
DOI	10.1007/s11802-021-4810-4
收录类别	SCI
语种	英语
资助项目	National Natural Science Foundation of China[31702386]; National Natural Science Foundation of China[31660251]; National Natural Science Foundation of China[31860245]; National Natural Science Foundation of China[31960203]; International Cooperation Science & Technology Planning Project of Guangdong Province of China[2017A050501037]; Natural Science Foundation of Guangxi Province[2018 GXNSFAA281019]; Natural Science Foundation of Guangxi Province[2017GXNSFAA198010]; Central Government Directs Special Funds for Local Science and Technology Development Projects[ZY1949 015]; Ministry of Science and Technology of Thailand; Mahasarakham University
WOS研究方向	Oceanography
WOS类目	Oceanography
WOS记录号	WOS:000682662400025
出版者	OCEAN UNIV CHINA
引用统计	被引频次：1[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/175981
专题	实验海洋生物学重点实验室
通讯作者	Wang Bei
作者单位	1.Guangdong Ocean Univ, Coll Fishery, Guangdong Prov Key Lab Pathogen Biol & Epidemiol, Key Lab Control Dis Aquat Anim Guangdong Higher E, Zhanjiang 524088, Peoples R China 2.Guangxi Acad Sci, State Key Lab Nonfood Biomass & Enzyme Technol, Natl Engn Res Ctr Nonfood Biorefinery, Nanning 536000, Peoples R China 3.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 4.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266237, Peoples R China 5.Mahasarakham Univ, Fac Technol, Dept Agr Technol, Div Fisheries,Res Unit Excellence Trop Fisheries, Kantarawichai, Mahasarakham, Thailand 6.Guangxi Acad Sci, Guangxi Beibu Gulf Marine Res Ctr, Guangxi Key Lab Marine Nat Prod & Combinatorial B, Nanning 536000, Peoples R China
通讯作者单位	实验海洋生物学重点实验室
推荐引用方式 GB/T 7714	Fan Bolin,Pan Lixia,Wang Zhongliang,et al. The Streptococcus agalactiae Ribose Binding Protein B (RbsB) Mediates Quorum Sensing Signal Uptake via Interaction with Autoinducer-2 Signals[J]. JOURNAL OF OCEAN UNIVERSITY OF CHINA,2021,20(5):1285-1295.
APA	Fan Bolin.,Pan Lixia.,Wang Zhongliang.,Eakapol, Wangkahart.,Huang Yuchong.,...&Wang Bei.(2021).The Streptococcus agalactiae Ribose Binding Protein B (RbsB) Mediates Quorum Sensing Signal Uptake via Interaction with Autoinducer-2 Signals.JOURNAL OF OCEAN UNIVERSITY OF CHINA,20(5),1285-1295.
MLA	Fan Bolin,et al."The Streptococcus agalactiae Ribose Binding Protein B (RbsB) Mediates Quorum Sensing Signal Uptake via Interaction with Autoinducer-2 Signals".JOURNAL OF OCEAN UNIVERSITY OF CHINA 20.5(2021):1285-1295.

条目包含的文件
文件名称/大小	文献类型	版本类型	开放类型	使用许可
Fan2021_Article_TheS（675KB）	期刊论文	出版稿	限制开放	CC BY-NC-SA	浏览