Pseudomonas aeruginosa Cryptic Prophage Endolysin Is a Highly Active Muramidase.

IF 2.9 3区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Per Kristian Thorén Edvardsen, Andrea Nikoline Englund, Åsmund Kjendseth Ro̷hr, Stéphane Mesnage, Gustav Vaaje-Kolstad
{"title":"<i>Pseudomonas aeruginosa</i> Cryptic Prophage Endolysin Is a Highly Active Muramidase.","authors":"Per Kristian Thorén Edvardsen, Andrea Nikoline Englund, Åsmund Kjendseth Ro̷hr, Stéphane Mesnage, Gustav Vaaje-Kolstad","doi":"10.1021/acs.biochem.5c00142","DOIUrl":null,"url":null,"abstract":"<p><p>Endolysins are phage-encoded enzymes that cleave the peptidoglycan of host bacteria. These enzymes have gained considerable attention due to their ability to cause cell lysis, making them candidates as antibacterial agents. Most <i><i>Pseudomonas aeruginosa</i></i> genomes, including the common laboratory strains PAO1 and UCBPP-PA14, contain a cryptic prophage encoding a glycoside hydrolase family 19 endolysin (named <i>Pa</i>GH19Lys in the present study). Family 19 glycoside hydrolases are known to target peptidoglycan and chitin-type substrates. <i>Pa</i>GH19Lys was not active toward chitin but exhibited activity toward chloroform-treated Gram-negative bacteria, displaying ∼10,000-fold higher activity than hen egg white lysozyme. Analysis of products derived from <i>Pa</i>GH19Lys activity toward purified <i><i>P. aeruginosa</i></i> peptidoglycan showed that the enzyme catalyzed hydrolysis of the β-1,4 linkage between <i>N-</i>acetylmuramic acid and <i>N-</i>acetyl-d-glucosamine, classifying the enzyme as a muramidase. Finally, the crystal structure of <i>Pa</i>GH19Lys was determined and solved to 1.8 Å resolution. The structure of the enzyme showed a globular α-helical fold possessing a deep but relatively open catalytic cleft.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":""},"PeriodicalIF":2.9000,"publicationDate":"2025-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry Biochemistry","FirstCategoryId":"1","ListUrlMain":"https://doi.org/10.1021/acs.biochem.5c00142","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Endolysins are phage-encoded enzymes that cleave the peptidoglycan of host bacteria. These enzymes have gained considerable attention due to their ability to cause cell lysis, making them candidates as antibacterial agents. Most Pseudomonas aeruginosa genomes, including the common laboratory strains PAO1 and UCBPP-PA14, contain a cryptic prophage encoding a glycoside hydrolase family 19 endolysin (named PaGH19Lys in the present study). Family 19 glycoside hydrolases are known to target peptidoglycan and chitin-type substrates. PaGH19Lys was not active toward chitin but exhibited activity toward chloroform-treated Gram-negative bacteria, displaying ∼10,000-fold higher activity than hen egg white lysozyme. Analysis of products derived from PaGH19Lys activity toward purified P. aeruginosa peptidoglycan showed that the enzyme catalyzed hydrolysis of the β-1,4 linkage between N-acetylmuramic acid and N-acetyl-d-glucosamine, classifying the enzyme as a muramidase. Finally, the crystal structure of PaGH19Lys was determined and solved to 1.8 Å resolution. The structure of the enzyme showed a globular α-helical fold possessing a deep but relatively open catalytic cleft.

铜绿假单胞菌隐前噬菌体内溶素是一种高活性的酶。
内溶酶是噬菌体编码的酶,可以切割宿主细菌的肽聚糖。这些酶由于其引起细胞裂解的能力而获得了相当大的关注,使它们成为抗菌剂的候选者。大多数铜绿假单胞菌基因组,包括常见的实验室菌株PAO1和UCBPP-PA14,都含有一个编码糖苷水解酶家族19内溶素的隐前噬菌体(本研究命名为PaGH19Lys)。已知19家族糖苷水解酶针对肽聚糖和几丁质型底物。PaGH19Lys对几丁质没有活性,但对氯仿处理的革兰氏阴性菌有活性,其活性比蛋清溶菌酶高1万倍。对纯化的P. aeruginosa肽聚糖的活性分析表明,PaGH19Lys酶催化了n -乙酰氨基乙酸和n -乙酰-d-葡萄糖胺之间的β-1,4键的水解,将该酶归类为酶酰胺酶。最后,对PaGH19Lys的晶体结构进行了测定,并求解到1.8 Å分辨率。酶的结构为球状α-螺旋结构,具有较深但相对开放的催化裂孔。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Biochemistry Biochemistry
Biochemistry Biochemistry 生物-生化与分子生物学
CiteScore
5.50
自引率
3.40%
发文量
336
审稿时长
1-2 weeks
期刊介绍: Biochemistry provides an international forum for publishing exceptional, rigorous, high-impact research across all of biological chemistry. This broad scope includes studies on the chemical, physical, mechanistic, and/or structural basis of biological or cell function, and encompasses the fields of chemical biology, synthetic biology, disease biology, cell biology, nucleic acid biology, neuroscience, structural biology, and biophysics. In addition to traditional Research Articles, Biochemistry also publishes Communications, Viewpoints, and Perspectives, as well as From the Bench articles that report new methods of particular interest to the biological chemistry community.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信