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噬菌体φAB6携带的解聚酶对抗生物膜形成和感染。

Phage φAB6-Borne Depolymerase Combats Biofilm Formation and Infection.

作者信息

Shahed-Al-Mahmud Md, Roy Rakesh, Sugiokto Febri Gunawan, Islam Md Nazmul, Lin Ming-Der, Lin Ling-Chun, Lin Nien-Tsung

机构信息

Master Program in Microbiology and Immunology, School of Medicine, Tzu Chi University, No. 701, Sec. 3, Zhongyang Rd., Hualien 97004, Taiwan.

Institute of Medical Sciences, Tzu Chi University, No. 701, Sec. 3, Zhongyang Rd., Hualien 97004, Taiwan.

出版信息

Antibiotics (Basel). 2021 Mar 9;10(3):279. doi: 10.3390/antibiotics10030279.

DOI:10.3390/antibiotics10030279
PMID:33803296
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7998257/
Abstract

Biofilm formation is one of the main causes of increased antibiotic resistance in infections. Bacteriophages and their derivatives, such as tail proteins with depolymerase activity, have shown considerable potential as antibacterial or antivirulence agents against bacterial infections. Here, we gained insights into the activity of a capsular polysaccharide (CPS) depolymerase, derived from the tailspike protein (TSP) of φAB6 phage, to degrade biofilm in vitro. Recombinant TSP showed enzymatic activity and was able to significantly inhibit biofilm formation and degrade formed biofilms; as low as 0.78 ng, the inhibition zone can still be formed on the bacterial lawn. Additionally, TSP inhibited the colonization of on the surface of Foley catheter sections, indicating that it can be used to prevent the adhesion of to medical device surfaces. Transmission and scanning electron microscopy demonstrated membrane leakage of bacterial cells treated with TSP, resulting in cell death. The therapeutic effect of TSP in zebrafish was also evaluated and the results showed that the survival rate was significantly improved (80%) compared with that of the untreated control group (10%). Altogether, we show that TSP derived from φAB6 is expected to become a new antibiotic against multi-drug resistant and a biocontrol agent that prevents the formation of biofilms on medical devices.

摘要

生物膜形成是感染中抗生素耐药性增加的主要原因之一。噬菌体及其衍生物,如具有解聚酶活性的尾蛋白,已显示出作为抗细菌感染的抗菌或抗毒力剂的巨大潜力。在此,我们深入了解了源自φAB6噬菌体尾刺蛋白(TSP)的荚膜多糖(CPS)解聚酶在体外降解生物膜的活性。重组TSP显示出酶活性,能够显著抑制生物膜形成并降解已形成的生物膜;低至0.78 ng时,仍可在细菌菌苔上形成抑菌圈。此外,TSP抑制了[细菌名称]在Foley导管切片表面的定植,表明它可用于防止[细菌名称]粘附于医疗设备表面。透射电子显微镜和扫描电子显微镜显示,用TSP处理的细菌细胞出现膜渗漏,导致细胞死亡。还评估了TSP在斑马鱼中的治疗效果,结果表明,与未处理的对照组(10%)相比,存活率显著提高(80%)。总之,我们表明源自φAB6的TSP有望成为一种针对多重耐药[细菌名称]的新型抗生素以及一种防止医疗设备上生物膜形成的生物防治剂。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/4a51df858819/antibiotics-10-00279-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/436c0e816f5e/antibiotics-10-00279-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/edabe21c8fbe/antibiotics-10-00279-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/33f8bedd3a93/antibiotics-10-00279-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/130b5ccc0531/antibiotics-10-00279-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/1c94ca0d84de/antibiotics-10-00279-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/5c4914cef45f/antibiotics-10-00279-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/277939847c86/antibiotics-10-00279-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/4a140daf3d3d/antibiotics-10-00279-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/4a51df858819/antibiotics-10-00279-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/436c0e816f5e/antibiotics-10-00279-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/edabe21c8fbe/antibiotics-10-00279-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/33f8bedd3a93/antibiotics-10-00279-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/130b5ccc0531/antibiotics-10-00279-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/1c94ca0d84de/antibiotics-10-00279-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/5c4914cef45f/antibiotics-10-00279-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/277939847c86/antibiotics-10-00279-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/4a140daf3d3d/antibiotics-10-00279-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2f8d/7998257/4a51df858819/antibiotics-10-00279-g009.jpg

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Mechanisms of Acinetobacter baumannii Capsular Polysaccharide Cleavage by Phage Depolymerases.
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