{"title":"下一个抗生素会从细菌中出现吗?","authors":"B. Labib","doi":"10.15173/sciential.v1i2.2094","DOIUrl":null,"url":null,"abstract":"An intrinsic bacterial mechanism could play a fundamental role in the future of antibiotics. Using cryo-EM, the structural resolution of the effector protein complexed with its chaperone and other accessory proteins reveals the mechanism of action of type VI bacterial secretion system. The importance of the chaperone protein, used to prime the toxic effector protein, was previously identified. Future research efforts should encompass the immunity protein that may allow bacteria to evade the lethal effects of this mechanism.","PeriodicalId":262888,"journal":{"name":"Sciential - McMaster Undergraduate Science Journal","volume":"59 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2019-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Could the Next Antibiotic Emerge from Bacteria?\",\"authors\":\"B. Labib\",\"doi\":\"10.15173/sciential.v1i2.2094\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"An intrinsic bacterial mechanism could play a fundamental role in the future of antibiotics. Using cryo-EM, the structural resolution of the effector protein complexed with its chaperone and other accessory proteins reveals the mechanism of action of type VI bacterial secretion system. The importance of the chaperone protein, used to prime the toxic effector protein, was previously identified. Future research efforts should encompass the immunity protein that may allow bacteria to evade the lethal effects of this mechanism.\",\"PeriodicalId\":262888,\"journal\":{\"name\":\"Sciential - McMaster Undergraduate Science Journal\",\"volume\":\"59 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-03-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Sciential - McMaster Undergraduate Science Journal\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15173/sciential.v1i2.2094\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Sciential - McMaster Undergraduate Science Journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15173/sciential.v1i2.2094","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
An intrinsic bacterial mechanism could play a fundamental role in the future of antibiotics. Using cryo-EM, the structural resolution of the effector protein complexed with its chaperone and other accessory proteins reveals the mechanism of action of type VI bacterial secretion system. The importance of the chaperone protein, used to prime the toxic effector protein, was previously identified. Future research efforts should encompass the immunity protein that may allow bacteria to evade the lethal effects of this mechanism.