The guanylate-binding protein GBP1 forms a protein coat that enwraps cytosol-invasive bacteria

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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.

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鸟苷酸结合蛋白 GBP1 形成包裹细胞膜入侵细菌的蛋白外衣
GBP1 是一种重要的先天性免疫成分,有助于控制细胞膜侵入性细菌病原体。我们利用低温电子显微镜(cryo-EM)、低温电子断层扫描(cryo-ET)和生物物理实验,展示了 GBP1 寡聚体如何包裹和重塑革兰氏阴性细菌病原体的含脂多糖(LPS)膜。
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Membrane structure-responsive lipid scrambling by TMEM63B to control plasma membrane lipid distribution Mechanism of polyadenylation-independent RNA polymerase II termination Time-course remodeling and pathology intervention of α-synuclein amyloid fibril by heparin and heparin-like oligosaccharides The guanylate-binding protein GBP1 forms a protein coat that enwraps cytosol-invasive bacteria Structural basis of antimicrobial membrane coat assembly by human GBP1
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