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形态不同的噬菌体PP99和PP101:噬菌体PP99尾刺蛋白对O-多糖的去乙酰化作用伴随感染过程。

Morphologically Different Bacteriophages PP99 and PP101: Deacetylation of O-Polysaccharide by the Tail Spike Protein of Phage PP99 Accompanies the Infection.

作者信息

Lukianova Anna A, Shneider Mikhail M, Evseev Peter V, Shpirt Anna M, Bugaeva Eugenia N, Kabanova Anastasia P, Obraztsova Ekaterina A, Miroshnikov Kirill K, Senchenkova Sofiya N, Shashkov Alexander S, Toschakov Stepan V, Knirel Yuriy A, Ignatov Alexander N, Miroshnikov Konstantin A

机构信息

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.

Department of Biology, Lomonosov Moscow State University, Moscow, Russia.

出版信息

Front Microbiol. 2020 Jan 23;10:3147. doi: 10.3389/fmicb.2019.03147. eCollection 2019.

Abstract

Soft rot caused by numerous species of and is a serious threat to the world production of potatoes. The application of bacteriophages to combat bacterial infections in medicine, agriculture, and the food industry requires the selection of comprehensively studied lytic phages and the knowledge of their infection mechanism for more rational composition of therapeutic cocktails. We present the study of two bacteriophages, infective for the strain F152. PP99 is a representative of the genus , and PP101 belongs to the still unclassified genomic group. The structure of O-polysaccharide of F152 was established by sugar analysis and 1D and 2D NMR spectroscopy: → 4)-α-D-Man6Ac-(1→ 2)-α-D-Man-(1→ 3)-β-D-Gal-(1→ The recombinant tail spike protein of phage PP99, gp55, was shown to deacetylate the side chain talose residue of bacterial O-polysaccharide, thus providing the selective attachment of the phage to the cell surface. Both phages demonstrate lytic behavior, thus being prospective for therapeutic purposes.

摘要

由多种 和 引起的软腐病对全球马铃薯生产构成严重威胁。在医学、农业和食品工业中应用噬菌体对抗细菌感染,需要选择经过全面研究的裂解性噬菌体,并了解其感染机制,以便更合理地配制治疗性混合制剂。我们展示了对两种能感染 菌株F152的噬菌体的研究。PP99是 属的代表,而PP101属于尚未分类的基因组群。通过糖分析以及一维和二维核磁共振光谱确定了F152的O-多糖结构:→ 4)-α-D-甘露糖醛酸-(1→ 2)-α-D-甘露糖-(1→ 3)-β-D-半乳糖-(1→ 噬菌体PP99的重组尾刺蛋白gp55可使细菌O-多糖的侧链塔罗糖残基脱乙酰化,从而使噬菌体选择性附着于细胞表面。两种噬菌体均表现出裂解行为,因此在治疗方面具有应用前景。

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