气候变化领域集成服务门户(CCPortal): The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid

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DOI	10.1073/pnas.2014442118
	The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid
	Salinas N.; Tayeb-Fligelman E.; Sammito M.D.; Bloch D.; Jelinek R.; Noy D.; Usón I.; Landau M.
发表日期	2021
ISSN	00278424
卷号	118 期号:3
英文摘要	Antimicrobial activity is being increasingly linked to amyloid fibril formation, suggesting physiological roles for some human amyloids, which have historically been viewed as strictly pathological agents. This work reports on formation of functional cross-α amyloid fibrils of the amphibian antimicrobial peptide uperin 3.5 at atomic resolution, an architecture initially discovered in the bacterial PSMα3 cytotoxin. The fibrils of uperin 3.5 and PSMα3 comprised antiparallel and parallel helical sheets, respectively, recapitulating properties of β-sheets. Uperin 3.5 demonstrated chameleon properties of a secondary structure switch, forming mostly cross-β fibrils in the absence of lipids. Uperin 3.5 helical fibril formation was largely induced by, and formed on, bacterial cells or membrane mimetics, and led to membrane damage and cell death. These findings suggest a regulation mechanism, which includes storage of inactive peptides as well as environmentally induced activation of uperin 3.5, via chameleon cross-α/β amyloid fibrils. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Amyloid; Antimicrobial peptides; Cross-alpha; Functional fibril
语种	英语
scopus关键词	amyloid; antimicrobial peptide uperin 3.5; polypeptide antibiotic agent; unclassified drug; antimicrobial activity; Article; cell death; collagen fibril; crystal structure; membrane damage; nonhuman; priority journal; protein cross linking; protein function; protein structure; Staphylococcus aureus
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/180961
作者单位	Department of Biology, Technion - Israel Institute of Technology, Haifa, 3200003, Israel; Crystallographic Methods, Institute of Molecular Biology of Barcelona−Spanish Research Council, Barcelona, 08028, Spain; Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva, 84105, Israel; Ilse Katz Institute for Nanotechnology, Ben Gurion University of the Negev, Beer Sheva, 84105, Israel; Migal-Galilee Research Institute, Kiryat Shmona, 1101602, Israel; Faculty of Sciences and Technology, Tel-Hai Academic College, Upper Galilee, 1220800, Israel; ICREA. Institució, Catalana de Recerca i Estudis Avançats, Barcelona, 08003, Spain; Centre for Structural Systems Biology, Hamburg, 22607, Germany; European Molecular Biology Laboratory (EMBL), Hamburg, 22607, Germany
推荐引用方式 GB/T 7714	Salinas N.,Tayeb-Fligelman E.,Sammito M.D.,et al. The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid[J],2021,118(3).
APA	Salinas N..,Tayeb-Fligelman E..,Sammito M.D..,Bloch D..,Jelinek R..,...&Landau M..(2021).The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid.Proceedings of the National Academy of Sciences of the United States of America,118(3).
MLA	Salinas N.,et al."The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid".Proceedings of the National Academy of Sciences of the United States of America 118.3(2021).