Characterization of the Pseudomonas aeruginosa T6SS PldB immunity proteins PA5086, PA5087 and PA5088 explains a novel stockpiling mechanism.,Acta Crystallographica Section F

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Characterization of the Pseudomonas aeruginosa T6SS PldB immunity proteins PA5086, PA5087 and PA5088 explains a novel stockpiling mechanism.
Acta Crystallographica Section F ( IF 1.1 ) Pub Date : 2020-05-01 , DOI: 10.1107/s2053230x2000566x
Haiying Wen ₁ , Zhi Geng ₂ , Zengqiang Gao ₂ , Zhun She ₂ , Yuhui Dong ₂

Affiliation

The bacterial type VI secretion system (T6SS) secretes many toxic effectors to gain advantage in interbacterial competition and for eukaryotic host infection. The cognate immunity proteins of these effectors protect bacteria from their own effectors. PldB is a T6SS trans‐kingdom effector in Pseudomonas aeruginosa that can infect both prokaryotic and eukaryotic cells. Three proteins, PA5086, PA5087 and PA5088, are employed to suppress the toxicity of PldB‐family proteins. The structures of PA5087 and PA5088 have previously been reported, but the identification of further distinctions between these immunity proteins is needed. Here, the crystal structure of PA5086 is reported at 1.90 Å resolution. A structural comparison of the three PldB immunity proteins showed vast divergences in their electrostatic potential surfaces. This interesting phenomenon provides an explanation of the stockpiling mechanism of T6SS immunity proteins.

中文翻译：

铜绿假单胞菌 T6SS PldB 免疫蛋白 PA5086、PA5087 和 PA5088 的表征解释了一种新的储存机制。

细菌 VI 型分泌系统 (T6SS) 分泌许多有毒效应物，以在细菌间竞争和真核宿主感染中获得优势。这些效应子的同源免疫蛋白保护细菌免受其自身效应子的侵害。PldB是铜绿假单胞菌中的T6SS跨界效应子，可以感染原核和真核细胞。三种蛋白 PA5086、PA5087 和 PA5088 用于抑制 PldB 家族蛋白的毒性。PA5087和PA5088的结构先前已被报道，但需要进一步鉴定这些免疫蛋白之间的区别。此处，PA5086 的晶体结构以 1.90 Å 分辨率报告。三种 PldB 免疫蛋白的结构比较显示，它们的静电势表面存在巨大差异。这一有趣的现象为 T6SS 免疫蛋白的储存机制提供了解释。

更新日期：2020-05-01

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