Georgina Benn, Carolina Borrelli, Dheeraj Prakaash, Alex N. T. Johnson, Vincent A. Fideli, Tahj Starr, Dylan Fitzmaurice, Ashton N. Combs, Martin Wühr, Enrique R. Rojas, Syma Khalid, Bart W. Hoogenboom, Thomas J. Silhavy
{"title":"OmpA控制外膜的秩序,分担机械负荷","authors":"Georgina Benn, Carolina Borrelli, Dheeraj Prakaash, Alex N. T. Johnson, Vincent A. Fideli, Tahj Starr, Dylan Fitzmaurice, Ashton N. Combs, Martin Wühr, Enrique R. Rojas, Syma Khalid, Bart W. Hoogenboom, Thomas J. Silhavy","doi":"10.1073/pnas.2416426121","DOIUrl":null,"url":null,"abstract":"OmpA, a predominant outer membrane (OM) protein in <jats:italic>Escherichia coli</jats:italic> , affects virulence, adhesion, and bacterial OM integrity. However, despite more than 50 y of research, the molecular basis for the role of OmpA has remained elusive. In this study, we demonstrate that OmpA organizes the OM protein lattice and mechanically connects it to the cell wall (CW). Using gene fusions, atomic force microscopy, simulations, and microfluidics, we show that the β-barrel domain of OmpA is critical for maintaining the permeability barrier, but both the β-barrel and CW–binding domains are necessary to enhance the cell envelope’s strength. OmpA integrates the compressive properties of the OM protein lattice with the tensile strength of the CW, forming a mechanically robust composite that increases overall integrity. This coupling likely underpins the ability of the entire envelope to function as a cohesive, resilient structure, critical for the survival of bacteria.","PeriodicalId":20548,"journal":{"name":"Proceedings of the National Academy of Sciences of the United States of America","volume":"21 1","pages":""},"PeriodicalIF":9.1000,"publicationDate":"2024-12-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"OmpA controls order in the outer membrane and shares the mechanical load\",\"authors\":\"Georgina Benn, Carolina Borrelli, Dheeraj Prakaash, Alex N. T. Johnson, Vincent A. Fideli, Tahj Starr, Dylan Fitzmaurice, Ashton N. Combs, Martin Wühr, Enrique R. Rojas, Syma Khalid, Bart W. Hoogenboom, Thomas J. Silhavy\",\"doi\":\"10.1073/pnas.2416426121\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"OmpA, a predominant outer membrane (OM) protein in <jats:italic>Escherichia coli</jats:italic> , affects virulence, adhesion, and bacterial OM integrity. However, despite more than 50 y of research, the molecular basis for the role of OmpA has remained elusive. In this study, we demonstrate that OmpA organizes the OM protein lattice and mechanically connects it to the cell wall (CW). Using gene fusions, atomic force microscopy, simulations, and microfluidics, we show that the β-barrel domain of OmpA is critical for maintaining the permeability barrier, but both the β-barrel and CW–binding domains are necessary to enhance the cell envelope’s strength. OmpA integrates the compressive properties of the OM protein lattice with the tensile strength of the CW, forming a mechanically robust composite that increases overall integrity. This coupling likely underpins the ability of the entire envelope to function as a cohesive, resilient structure, critical for the survival of bacteria.\",\"PeriodicalId\":20548,\"journal\":{\"name\":\"Proceedings of the National Academy of Sciences of the United States of America\",\"volume\":\"21 1\",\"pages\":\"\"},\"PeriodicalIF\":9.1000,\"publicationDate\":\"2024-12-04\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Proceedings of the National Academy of Sciences of the United States of America\",\"FirstCategoryId\":\"103\",\"ListUrlMain\":\"https://doi.org/10.1073/pnas.2416426121\",\"RegionNum\":1,\"RegionCategory\":\"综合性期刊\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"MULTIDISCIPLINARY SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proceedings of the National Academy of Sciences of the United States of America","FirstCategoryId":"103","ListUrlMain":"https://doi.org/10.1073/pnas.2416426121","RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
OmpA controls order in the outer membrane and shares the mechanical load
OmpA, a predominant outer membrane (OM) protein in Escherichia coli , affects virulence, adhesion, and bacterial OM integrity. However, despite more than 50 y of research, the molecular basis for the role of OmpA has remained elusive. In this study, we demonstrate that OmpA organizes the OM protein lattice and mechanically connects it to the cell wall (CW). Using gene fusions, atomic force microscopy, simulations, and microfluidics, we show that the β-barrel domain of OmpA is critical for maintaining the permeability barrier, but both the β-barrel and CW–binding domains are necessary to enhance the cell envelope’s strength. OmpA integrates the compressive properties of the OM protein lattice with the tensile strength of the CW, forming a mechanically robust composite that increases overall integrity. This coupling likely underpins the ability of the entire envelope to function as a cohesive, resilient structure, critical for the survival of bacteria.
期刊介绍:
The Proceedings of the National Academy of Sciences (PNAS), a peer-reviewed journal of the National Academy of Sciences (NAS), serves as an authoritative source for high-impact, original research across the biological, physical, and social sciences. With a global scope, the journal welcomes submissions from researchers worldwide, making it an inclusive platform for advancing scientific knowledge.