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DING 蛋白在铜绿假单胞菌含 PstS 的外表面附属物上的定位。

Localization of DING proteins on PstS-containing outer-surface appendages of Pseudomonas aeruginosa.

机构信息

School of Biological Sciences, University of Auckland, Auckland, New Zealand; Department of Surgery, Pritzker School of Medicine, University of Chicago, Chicago, IL, USA.

出版信息

FEMS Microbiol Lett. 2014 Mar;352(1):54-61. doi: 10.1111/1574-6968.12368. Epub 2014 Jan 21.

Abstract

Phosphate signaling and acquisition are critical for the bacterial response to phosphate limitation, and bacteria express multiple factors to scavenge phosphate. We previously found that multidrug-resistant strains of Pseudomonas aeruginosa from critically ill patients can form unusual outer-surface appendages harboring PstS proteins. Here, we have expanded our investigation to DING proteins that like PstS belong to the family of high-affinity phosphate-binding proteins but have strong similarity with eukaryotic DING proteins. We demonstrate the localization of DING on PstS-containing outer-surface appendages in both multidrug-resistant strain MDR25 and the PA14 strain of P. aeruginosa. However, the number of cells producing appendages and the amount of appendages on each cell in PA14 were found to be negligible, unless overexpression of either PstS or DING was achieved by transformation with constructed plasmids. We further noticed that DING expression under low phosphate conditions was significantly higher in MDR25 compared to PA14 which may explain the greater abundance of appendages in MDR25. Our finding that DING proteins are localized on extracellular appendages provides an opportunity to study the interaction of bacterial DING with host proteins by mimicking the action of host DINGs.

摘要

磷酸盐信号转导和获取对于细菌对磷酸盐限制的反应至关重要,细菌表达多种因子来掠夺磷酸盐。我们之前发现,来自重症患者的多药耐药铜绿假单胞菌菌株可以形成携带 PstS 蛋白的不寻常的外表面附属物。在这里,我们扩展了我们的研究范围,研究了 DING 蛋白,这些蛋白与 PstS 一样属于高亲和力磷酸盐结合蛋白家族,但与真核 DING 蛋白具有很强的相似性。我们证明了 DING 在含有 PstS 的外表面附属物上的定位,无论是在多药耐药株 MDR25 还是铜绿假单胞菌 PA14 菌株中。然而,发现只有在通过构建质粒转化实现 PstS 或 DING 的过表达时,PA14 中产生附属物的细胞数量和每个细胞上的附属物数量才可以忽略不计。我们进一步注意到,在低磷酸盐条件下,MDR25 中的 DING 表达明显高于 PA14,这可能解释了 MDR25 中附属物更丰富的原因。我们发现 DING 蛋白定位于细胞外附属物上,为通过模拟宿主 DING 的作用来研究细菌 DING 与宿主蛋白的相互作用提供了机会。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/98bd/4237115/4d8120a19b28/fml0352-0054-f1.jpg

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