{"title":"鸟苷酸结合蛋白 GBP1 形成包裹细胞膜入侵细菌的蛋白外衣","authors":"","doi":"10.1038/s41594-024-01403-6","DOIUrl":null,"url":null,"abstract":"GBP1 is an important innate immunity component that contributes to the control of cytosol-invasive bacterial pathogens. Using cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET) and biophysical assays, we show how GBP1 oligomers enwrap and remodel the lipopolysaccharide (LPS)-containing membrane of gram-negative bacterial pathogens.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 1","pages":"8-9"},"PeriodicalIF":12.5000,"publicationDate":"2024-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The guanylate-binding protein GBP1 forms a protein coat that enwraps cytosol-invasive bacteria\",\"authors\":\"\",\"doi\":\"10.1038/s41594-024-01403-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"GBP1 is an important innate immunity component that contributes to the control of cytosol-invasive bacterial pathogens. Using cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET) and biophysical assays, we show how GBP1 oligomers enwrap and remodel the lipopolysaccharide (LPS)-containing membrane of gram-negative bacterial pathogens.\",\"PeriodicalId\":49141,\"journal\":{\"name\":\"Nature Structural & Molecular Biology\",\"volume\":\"32 1\",\"pages\":\"8-9\"},\"PeriodicalIF\":12.5000,\"publicationDate\":\"2024-10-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature Structural & Molecular Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.nature.com/articles/s41594-024-01403-6\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature Structural & Molecular Biology","FirstCategoryId":"99","ListUrlMain":"https://www.nature.com/articles/s41594-024-01403-6","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
The guanylate-binding protein GBP1 forms a protein coat that enwraps cytosol-invasive bacteria
GBP1 is an important innate immunity component that contributes to the control of cytosol-invasive bacterial pathogens. Using cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET) and biophysical assays, we show how GBP1 oligomers enwrap and remodel the lipopolysaccharide (LPS)-containing membrane of gram-negative bacterial pathogens.
期刊介绍:
Nature Structural & Molecular Biology is a comprehensive platform that combines structural and molecular research. Our journal focuses on exploring the functional and mechanistic aspects of biological processes, emphasizing how molecular components collaborate to achieve a particular function. While structural data can shed light on these insights, our publication does not require them as a prerequisite.