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The Streptococcus agalactiae Ribose Binding Protein B (RbsB) Mediates Quorum Sensing Signal Uptake via Interaction with Autoinducer-2 Signals
Fan Bolin1; Pan Lixia2; Wang Zhongliang1; Eakapol, Wangkahart5; Huang Yuchong1,3,4; Yang Dengfeng6; Jian Jichang1,3,4; Huang Yu1,3,4; Wang Bei1,3,4
2021-10-01
Source PublicationJOURNAL OF OCEAN UNIVERSITY OF CHINA
ISSN1672-5182
Volume20Issue:5Pages:1285-1295
Corresponding AuthorWang Bei(wong19820204@126.com)
AbstractUnderstanding 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.
KeywordStreptococcus agalactiae RbsB protein circular dichroism (CD) spectroscopy isothermal titration calorimetry(200) (ITC200) molecular docking
DOI10.1007/s11802-021-4810-4
Indexed BySCI
Language英语
Funding ProjectNational 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 Research AreaOceanography
WOS SubjectOceanography
WOS IDWOS:000682662400025
PublisherOCEAN UNIV CHINA
Citation statistics
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/175981
Collection实验海洋生物学重点实验室
Corresponding AuthorWang Bei
Affiliation1.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
Corresponding Author AffilicationKey Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
Recommended Citation
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.
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