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抗菌肺蛋白对 … 的协同作用。

Synergistic Action of Antimicrobial Lung Proteins against .

机构信息

Department of Biochemistry and Molecular Biology, Complutense University of Madrid, 28040 Madrid, Spain.

Division of Pulmonary Biology, Cincinnati Children's Hospital Medical Center and University of Cincinnati College of Medicine, Cincinnati, OH 45229, USA.

出版信息

Int J Mol Sci. 2021 Oct 15;22(20):11146. doi: 10.3390/ijms222011146.

DOI:10.3390/ijms222011146
PMID:34681806
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8538444/
Abstract

As key components of innate immunity, lung antimicrobial proteins play a critical role in warding off invading respiratory pathogens. Lung surfactant protein A (SP-A) exerts synergistic antimicrobial activity with the -terminal segment of the SP-B proprotein (SP-B) against K2 in vivo. However, the factors that govern SP-A/SP-B antimicrobial activity are still unclear. The aim of this study was to identify the mechanisms by which SP-A and SP-B act synergistically against , which is resistant to either protein alone. The effect of these proteins on was studied by membrane permeabilization and depolarization assays and transmission electron microscopy. Their effects on model membranes of the outer and inner bacterial membranes were analyzed by differential scanning calorimetry and membrane leakage assays. Our results indicate that the SP-A/SP-B complex alters the ultrastructure of by binding to lipopolysaccharide molecules present in the outer membrane, forming packing defects in the membrane that may favor the translocation of both proteins to the periplasmic space. The SP-A/SP-B complex depolarized and permeabilized the inner membrane, perhaps through the induction of toroidal pores. We conclude that the synergistic antimicrobial activity of SP-A/SP-B is based on the capability of this complex, but not either protein alone, to alter the integrity of bacterial membranes.

摘要

作为先天免疫的关键组成部分，肺部抗菌蛋白在抵御入侵呼吸道病原体方面发挥着至关重要的作用。肺表面活性蛋白 A（SP-A）与 SP-B 前蛋白的 - 末端段（SP-B）协同发挥抗微生物活性，针对体内 K2。然而，控制 SP-A/SP-B 抗微生物活性的因素仍不清楚。本研究旨在确定 SP-A 和 SP-B 协同作用对抗单独一种蛋白具有抗性的 的机制。通过膜通透性和去极化测定以及透射电子显微镜研究这些蛋白对 的影响。通过差示扫描量热法和膜渗漏测定分析它们对内外膜模型膜的影响。我们的结果表明，SP-A/SP-B 复合物通过与外膜中存在的脂多糖分子结合，改变 的超微结构，在膜中形成包装缺陷，这可能有利于两种蛋白向周质空间的易位。SP-A/SP-B 复合物去极化并破坏内膜，可能是通过诱导环形孔。我们的结论是，SP-A/SP-B 的协同抗微生物活性基于该复合物的能力，而不是单独的任何一种蛋白，改变细菌膜的完整性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/53f1/8538444/c1298ce6f180/ijms-22-11146-g009.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/53f1/8538444/674108279f33/ijms-22-11146-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/53f1/8538444/c1298ce6f180/ijms-22-11146-g009.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/53f1/8538444/8d9247398b13/ijms-22-11146-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/53f1/8538444/674108279f33/ijms-22-11146-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/53f1/8538444/c1298ce6f180/ijms-22-11146-g009.jpg

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