Rosie A. Waters, James Robinson, J. Michael Edwardson
{"title":"Syncollin是一种抗菌多肽","authors":"Rosie A. Waters, James Robinson, J. Michael Edwardson","doi":"10.1111/cmi.13372","DOIUrl":null,"url":null,"abstract":"<div>\n \n \n <section>\n \n <p>Syncollin is a 16-kDa protein found predominantly in the zymogen granules of pancreatic acinar cells, with expression at lower levels in intestinal epithelial cells and neutrophils. Here, we used Strep-tagged syncollin isolated from the supernatant of transiently transfected mammalian cells to test the hypothesis that syncollin has antibacterial properties, which might enable it to play a role in host defence in the gut and possibly elsewhere. We show that syncollin is an exceptionally thermostable protein with a circular dichroism spectrum consistent with a predominantly beta-sheet structure. Syncollin binds to bacterial peptidoglycan and restricts the growth of representative Gram-positive (<i>Lactococcus lactis</i>) and Gram-negative (<i>Escherichia coli</i>) bacteria. Syncollin induces propidium iodide uptake into <i>E. coli</i> (but not <i>L. lactis</i>), indicating permeabilisation of the bacterial membrane. It also causes surface structural damage in both <i>L. lactis</i> and <i>E. coli</i>, as visualised by scanning electron microscopy. We propose that syncollin is a previously unidentified member of a large group of antimicrobial polypeptides that control the gut microbiome.</p>\n </section>\n \n <section>\n \n <h3> Take Aways</h3>\n \n <div>\n <ul>\n \n <li>Syncollin is a 16-kDa protein found in pancreatic zymogen granules.</li>\n \n <li>Syncollin is highly thermostable and has a predominantly beta-sheet structure.</li>\n \n <li>Syncollin binds peptidoglycan and restricts the growth of <i>L. lactis</i> and <i>E. coli</i>.</li>\n \n <li>Syncollin causes propidium iodide uptake into <i>E. coli</i> (but not <i>L. lactis</i>).</li>\n \n <li>Syncollin causes surface structural damage in both <i>L. lactis</i> and <i>E. coli</i>.</li>\n </ul>\n </div>\n </section>\n </div>","PeriodicalId":9844,"journal":{"name":"Cellular Microbiology","volume":"23 10","pages":""},"PeriodicalIF":2.6000,"publicationDate":"2021-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13372","citationCount":"1","resultStr":"{\"title\":\"Syncollin is an antibacterial polypeptide\",\"authors\":\"Rosie A. Waters, James Robinson, J. Michael Edwardson\",\"doi\":\"10.1111/cmi.13372\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div>\\n \\n \\n <section>\\n \\n <p>Syncollin is a 16-kDa protein found predominantly in the zymogen granules of pancreatic acinar cells, with expression at lower levels in intestinal epithelial cells and neutrophils. Here, we used Strep-tagged syncollin isolated from the supernatant of transiently transfected mammalian cells to test the hypothesis that syncollin has antibacterial properties, which might enable it to play a role in host defence in the gut and possibly elsewhere. We show that syncollin is an exceptionally thermostable protein with a circular dichroism spectrum consistent with a predominantly beta-sheet structure. Syncollin binds to bacterial peptidoglycan and restricts the growth of representative Gram-positive (<i>Lactococcus lactis</i>) and Gram-negative (<i>Escherichia coli</i>) bacteria. Syncollin induces propidium iodide uptake into <i>E. coli</i> (but not <i>L. lactis</i>), indicating permeabilisation of the bacterial membrane. It also causes surface structural damage in both <i>L. lactis</i> and <i>E. coli</i>, as visualised by scanning electron microscopy. We propose that syncollin is a previously unidentified member of a large group of antimicrobial polypeptides that control the gut microbiome.</p>\\n </section>\\n \\n <section>\\n \\n <h3> Take Aways</h3>\\n \\n <div>\\n <ul>\\n \\n <li>Syncollin is a 16-kDa protein found in pancreatic zymogen granules.</li>\\n \\n <li>Syncollin is highly thermostable and has a predominantly beta-sheet structure.</li>\\n \\n <li>Syncollin binds peptidoglycan and restricts the growth of <i>L. lactis</i> and <i>E. coli</i>.</li>\\n \\n <li>Syncollin causes propidium iodide uptake into <i>E. coli</i> (but not <i>L. lactis</i>).</li>\\n \\n <li>Syncollin causes surface structural damage in both <i>L. lactis</i> and <i>E. coli</i>.</li>\\n </ul>\\n </div>\\n </section>\\n </div>\",\"PeriodicalId\":9844,\"journal\":{\"name\":\"Cellular Microbiology\",\"volume\":\"23 10\",\"pages\":\"\"},\"PeriodicalIF\":2.6000,\"publicationDate\":\"2021-06-21\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1111/cmi.13372\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cellular Microbiology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1111/cmi.13372\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CELL BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cellular Microbiology","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/cmi.13372","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
Syncollin is a 16-kDa protein found predominantly in the zymogen granules of pancreatic acinar cells, with expression at lower levels in intestinal epithelial cells and neutrophils. Here, we used Strep-tagged syncollin isolated from the supernatant of transiently transfected mammalian cells to test the hypothesis that syncollin has antibacterial properties, which might enable it to play a role in host defence in the gut and possibly elsewhere. We show that syncollin is an exceptionally thermostable protein with a circular dichroism spectrum consistent with a predominantly beta-sheet structure. Syncollin binds to bacterial peptidoglycan and restricts the growth of representative Gram-positive (Lactococcus lactis) and Gram-negative (Escherichia coli) bacteria. Syncollin induces propidium iodide uptake into E. coli (but not L. lactis), indicating permeabilisation of the bacterial membrane. It also causes surface structural damage in both L. lactis and E. coli, as visualised by scanning electron microscopy. We propose that syncollin is a previously unidentified member of a large group of antimicrobial polypeptides that control the gut microbiome.
Take Aways
Syncollin is a 16-kDa protein found in pancreatic zymogen granules.
Syncollin is highly thermostable and has a predominantly beta-sheet structure.
Syncollin binds peptidoglycan and restricts the growth of L. lactis and E. coli.
Syncollin causes propidium iodide uptake into E. coli (but not L. lactis).
Syncollin causes surface structural damage in both L. lactis and E. coli.
期刊介绍：
Cellular Microbiology aims to publish outstanding contributions to the understanding of interactions between microbes, prokaryotes and eukaryotes, and their host in the context of pathogenic or mutualistic relationships, including co-infections and microbiota. We welcome studies on single cells, animals and plants, and encourage the use of model hosts and organoid cultures. Submission on cell and molecular biological aspects of microbes, such as their intracellular organization or the establishment and maintenance of their architecture in relation to virulence and pathogenicity are also encouraged. Contributions must provide mechanistic insights supported by quantitative data obtained through imaging, cellular, biochemical, structural or genetic approaches.
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