The Streptococcus agalactiae Ribose Binding Protein B(RbsB)Mediates Quorum Sensing Signal Uptake via Interaction with Autoinducer-2 Signals
文献类型：CNKI期刊论文
| 作者 | FAN Bolin; PAN Lixia; WANG Zhongliang; WANGKAHART Eakapol; HUANG Yuchong; YANG Dengfeng; JIAN Jichang; HUANG Yu; WANG Bei
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| 发表日期 | 2021-10-06 |
| 出处 | Journal of Ocean University of China
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| 关键词 | Streptococcus agalactiae RbsB protein circular dichroism (CD) spectroscopy isothermal titration calorimetry_(200)(ITC_(200)) molecular docking |
| 英文摘要 | 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 Rbs B protein has similarity to Escherichia coli Lsr B and Aggregatibacter actinomycetemcomitans Rbs B proteins that bind AI-2.We hypothesized that Rbs B protein mediates quorum sensing signal uptake via interaction with AI-2.To evaluate the regulatory effect of Rbs B on QS system,the recombinant plasmid p GEX-6p-1-Rbs B was constructed and Rbs B protein was purified with GST-tag.To further elucidate the role of Rbs B protein binding to DPD (AI-2 precursor dihydroxypentanedione),the systematically throughput circular dichroism (CD) spectroscopy,isothermal titration calorimetry_(200) (ITC_(200)) and molecular docking methods were employed.The high expression of soluble Rbs B protein with molecular weight of 33 k Da was obtained.The thermodynamics results (ΔH<0,ΔS<0,ΔG<0) with ITC determination indicated that the binding process between DPD and Rbs B 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 Rbs B in a dose-dependent manner,suggesting that Rbs B was changed in the microenvironment of DPD when the DPD concentration was between 0.8–1.0 mmol L~(-1) and reaching the maximum binding amount.According to molecular docking,3hydrophobic residues involved in DPD and Rbs B protein stable binding were be found,and also hydrogen bonding plays a key role in the formation of the new complex.Rbs B 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 Rbs B may play a role in the response of S.agalactiace to AI-2. |
| 文献子类 | CNKI期刊论文 |
| 资助机构 | supported by the National Natural Science Foundation of China (Nos. 31702386, 31660251, 31860245 and 31960203) ; the International Cooperation Science & Technology Planning Project of Guangdong Province of China (No. 2017A050501037) ; the Natural Science Foundation of Guangxi Province (Nos. 2018 GXNSFAA281019, 2017GXNSFAA198010) ; the Central Government Directs Special Funds for Local Science and Technology Development Projects (No. ZY1949 015) ; supported financially by the Ministry of Science and Technology of Thailand and Mahasarakham University |
| 卷 | v.20期:05页:263-273 |
| 语种 | 英文; |
| 分类号 | S917.1 |
| ISSN号 | 1672-5182 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/187637]  |
| 专题 | 中国科学院海洋研究所 |
| 作者单位 | 1.ResearchUnitofExcellenceforTropicalFisheriesandTechnology,DivisionofFisheries,DepartmentofAgriculturalTechnology,FacultyofTechnology,MahasarakhamUniversity 2.CollegeofFishery,GuangdongOceanUniversity,GuangdongProvincialKeyLaboratoryofPathogenicBiologyandEpidemiologyforAquaticEconomicAnimal,KeyLaboratoryofControlforDiseaseofAquaticAnimalsofGuangdongHigherEducationInstitutes 3.NationalEngineeringResearchCenterforNon-FoodBiorefinery,StateKeyLaboratoryofNon-FoodBiomassandEnzymeTechnology,GuangxiAcademyofSciences 4.KeyLaboratoryofExperimentalMarineBiology,InstituteofOceanology,ChineseAcademyofSciences 5.LaboratoryforMarineBiologyandBiotechnology,QingdaoNationalLaboratoryforMarineScienceandTechnology 6.GuangxiKeyLaboratoryofMarineNaturalProductsandCombinatorialBiosynthesisChemistry,GuangxiBeibuGulfMarineResearchCenter,GuangxiAcademyofSciences |
| 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. 2021. |
入库方式： OAI收割
来源：海洋研究所
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