CCPortal
DOI10.1073/pnas.2101349118
Periscope Proteins are variable-length regulators of bacterial cell surface interactions
Whelan F.; Lafita A.; Gilburt J.; Dégut C.; Griffiths S.C.; Jenkins H.T.; St John A.N.; Paci E.; Moir J.W.B.; Plevin M.J.; Baumann C.G.; Bateman A.; Potts J.R.
发表日期2021
ISSN0027-8424
卷号118期号:23
英文摘要Changes at the cell surface enable bacteria to survive in dynamic environments, such as diverse niches of the human host. Here, we reveal “Periscope Proteins” as a widespread mechanism of bacterial surface alteration mediated through protein length variation. Tandem arrays of highly similar folded domains can form an elongated rod-like structure; thus, variation in the number of domains determines how far an N-terminal host ligand binding domain projects from the cell surface. Supported by newly available long-read genome sequencing data, we propose that this class could contain over 50 distinct proteins, including those implicated in host colonization and biofilm formation by human pathogens. In large multidomain proteins, sequence divergence between adjacent domains appears to reduce interdomain misfolding. Periscope Proteins break this “rule,” suggesting that their length variability plays an important role in regulating bacterial interactions with host surfaces, other bacteria, and the immune system. © This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY).
英文关键词Bacterial surface proteins; Multidomain proteins; Protein structure
语种英语
scopus关键词article; bacterial cell; biofilm; cell surface; human; immune system; ligand binding; protein domain
来源期刊Proceedings of the National Academy of Sciences of the United States of America
文献类型期刊论文
条目标识符http://gcip.llas.ac.cn/handle/2XKMVOVA/238898
作者单位Department of Biology, The University of York, York, YO10 5DD, United Kingdom; European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome CampusCB10 1SD, United Kingdom; Department of Chemistry, The University of York, York, YO10 5DD, United Kingdom; Astbury Centre for Structural Molecular Biology, The University of Leeds, Leeds, LS2 9JT, United Kingdom; Department of Molecular and Biomedical Science, The University of Adelaide, Adelaide, SA 5005, Australia; School of Life and Environmental Sciences, University of Sydney, Camperdown, NSW 2006, Australia
推荐引用方式
GB/T 7714
Whelan F.,Lafita A.,Gilburt J.,et al. Periscope Proteins are variable-length regulators of bacterial cell surface interactions[J],2021,118(23).
APA Whelan F..,Lafita A..,Gilburt J..,Dégut C..,Griffiths S.C..,...&Potts J.R..(2021).Periscope Proteins are variable-length regulators of bacterial cell surface interactions.Proceedings of the National Academy of Sciences of the United States of America,118(23).
MLA Whelan F.,et al."Periscope Proteins are variable-length regulators of bacterial cell surface interactions".Proceedings of the National Academy of Sciences of the United States of America 118.23(2021).
条目包含的文件
条目无相关文件。
个性服务
推荐该条目
保存到收藏夹
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Whelan F.]的文章
[Lafita A.]的文章
[Gilburt J.]的文章
百度学术
百度学术中相似的文章
[Whelan F.]的文章
[Lafita A.]的文章
[Gilburt J.]的文章
必应学术
必应学术中相似的文章
[Whelan F.]的文章
[Lafita A.]的文章
[Gilburt J.]的文章
相关权益政策
暂无数据
收藏/分享

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。