An investigation into the Omp85 protein BamK in hypervirulent Klebsiella pneumoniae, and its role in outer membrane biogenesis

Von Vergel L. Torres, Eva Heinz, Christopher J. Stubenrauch, Jonathan J. Wilksch, Hanwei Cao, Ji Yang, Abigail Clements, Rhys A. Dunstan, Felicity Alcock, Chaille T. Webb, G. Dougan, Richard A. Strugnell, Iain D. Hay, Trevor Lithgow

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Members of the Omp85 protein superfamily have important roles in Gram-negative bacteria, with the archetypal protein BamA being ubiquitous given its essential function in the assembly of outer membrane proteins. In some bacterial lineages, additional members of the family exist and, in most of these cases, the function of the protein is unknown. We detected one of these Omp85 proteins in the pathogen Klebsiella pneumoniae B5055, and refer to the protein as BamK. Here we show that bamK is a conserved element in the core genome of Klebsiella, and its expression rescues a loss-of-function DeltabamA mutant. We developed an E. coli model system to measure and compare the specific activity of BamA and BamK in the assembly reaction for the critical substrate LptD, and find that BamK is as efficient as BamA in assembling the native LptDE complex. Comparative structural analysis revealed that the major distinction between BamK and BamA is in the external facing surface of the protein, and we discuss how such changes may contribute to a mechanism for resistance against infection by bacteriophage. This article is protected by copyright. All rights reserved.
Original languageEnglish
Pages (from-to)584-599
Number of pages16
JournalMolecular Microbiology
Volume109
Issue number5
DOIs
Publication statusPublished - Sep 2018

Keywords

  • BAM complex
  • BamA
  • hypervirulence
  • cell wall
  • beta-barrel proteins

Cite this

Torres, Von Vergel L. ; Heinz, Eva ; Stubenrauch, Christopher J. ; Wilksch, Jonathan J. ; Cao, Hanwei ; Yang, Ji ; Clements, Abigail ; Dunstan, Rhys A. ; Alcock, Felicity ; Webb, Chaille T. ; Dougan, G. ; Strugnell, Richard A. ; Hay, Iain D. ; Lithgow, Trevor. / An investigation into the Omp85 protein BamK in hypervirulent Klebsiella pneumoniae, and its role in outer membrane biogenesis. In: Molecular Microbiology. 2018 ; Vol. 109, No. 5. pp. 584-599.
@article{0147dd66cd8d4e0ca02477da7e136d2d,
title = "An investigation into the Omp85 protein BamK in hypervirulent Klebsiella pneumoniae, and its role in outer membrane biogenesis",
abstract = "Members of the Omp85 protein superfamily have important roles in Gram-negative bacteria, with the archetypal protein BamA being ubiquitous given its essential function in the assembly of outer membrane proteins. In some bacterial lineages, additional members of the family exist and, in most of these cases, the function of the protein is unknown. We detected one of these Omp85 proteins in the pathogen Klebsiella pneumoniae B5055, and refer to the protein as BamK. Here we show that bamK is a conserved element in the core genome of Klebsiella, and its expression rescues a loss-of-function DeltabamA mutant. We developed an E. coli model system to measure and compare the specific activity of BamA and BamK in the assembly reaction for the critical substrate LptD, and find that BamK is as efficient as BamA in assembling the native LptDE complex. Comparative structural analysis revealed that the major distinction between BamK and BamA is in the external facing surface of the protein, and we discuss how such changes may contribute to a mechanism for resistance against infection by bacteriophage. This article is protected by copyright. All rights reserved.",
keywords = "BAM complex, BamA, hypervirulence, cell wall, beta-barrel proteins",
author = "Torres, {Von Vergel L.} and Eva Heinz and Stubenrauch, {Christopher J.} and Wilksch, {Jonathan J.} and Hanwei Cao and Ji Yang and Abigail Clements and Dunstan, {Rhys A.} and Felicity Alcock and Webb, {Chaille T.} and G. Dougan and Strugnell, {Richard A.} and Hay, {Iain D.} and Trevor Lithgow",
note = "Torres, Von Vergel L Heinz, Eva Stubenrauch, Christopher J Wilksch, Jonathan J Cao, Hanwei Yang, Ji Clements, Abigail Dunstan, Rhys A Alcock, Felicity Webb, Chaille T Dougan, Gordon Strugnell, Richard A Hay, Iain D Lithgow, Trevor eng England Mol Microbiol. 2018 Jun 5. doi: 10.1111/mmi.13990.",
year = "2018",
month = "9",
doi = "10.1111/mmi.13990",
language = "English",
volume = "109",
pages = "584--599",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley-Blackwell",
number = "5",

}

An investigation into the Omp85 protein BamK in hypervirulent Klebsiella pneumoniae, and its role in outer membrane biogenesis. / Torres, Von Vergel L.; Heinz, Eva; Stubenrauch, Christopher J.; Wilksch, Jonathan J.; Cao, Hanwei; Yang, Ji; Clements, Abigail; Dunstan, Rhys A.; Alcock, Felicity; Webb, Chaille T.; Dougan, G.; Strugnell, Richard A.; Hay, Iain D.; Lithgow, Trevor.

In: Molecular Microbiology, Vol. 109, No. 5, 09.2018, p. 584-599.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - An investigation into the Omp85 protein BamK in hypervirulent Klebsiella pneumoniae, and its role in outer membrane biogenesis

AU - Torres, Von Vergel L.

AU - Heinz, Eva

AU - Stubenrauch, Christopher J.

AU - Wilksch, Jonathan J.

AU - Cao, Hanwei

AU - Yang, Ji

AU - Clements, Abigail

AU - Dunstan, Rhys A.

AU - Alcock, Felicity

AU - Webb, Chaille T.

AU - Dougan, G.

AU - Strugnell, Richard A.

AU - Hay, Iain D.

AU - Lithgow, Trevor

N1 - Torres, Von Vergel L Heinz, Eva Stubenrauch, Christopher J Wilksch, Jonathan J Cao, Hanwei Yang, Ji Clements, Abigail Dunstan, Rhys A Alcock, Felicity Webb, Chaille T Dougan, Gordon Strugnell, Richard A Hay, Iain D Lithgow, Trevor eng England Mol Microbiol. 2018 Jun 5. doi: 10.1111/mmi.13990.

PY - 2018/9

Y1 - 2018/9

N2 - Members of the Omp85 protein superfamily have important roles in Gram-negative bacteria, with the archetypal protein BamA being ubiquitous given its essential function in the assembly of outer membrane proteins. In some bacterial lineages, additional members of the family exist and, in most of these cases, the function of the protein is unknown. We detected one of these Omp85 proteins in the pathogen Klebsiella pneumoniae B5055, and refer to the protein as BamK. Here we show that bamK is a conserved element in the core genome of Klebsiella, and its expression rescues a loss-of-function DeltabamA mutant. We developed an E. coli model system to measure and compare the specific activity of BamA and BamK in the assembly reaction for the critical substrate LptD, and find that BamK is as efficient as BamA in assembling the native LptDE complex. Comparative structural analysis revealed that the major distinction between BamK and BamA is in the external facing surface of the protein, and we discuss how such changes may contribute to a mechanism for resistance against infection by bacteriophage. This article is protected by copyright. All rights reserved.

AB - Members of the Omp85 protein superfamily have important roles in Gram-negative bacteria, with the archetypal protein BamA being ubiquitous given its essential function in the assembly of outer membrane proteins. In some bacterial lineages, additional members of the family exist and, in most of these cases, the function of the protein is unknown. We detected one of these Omp85 proteins in the pathogen Klebsiella pneumoniae B5055, and refer to the protein as BamK. Here we show that bamK is a conserved element in the core genome of Klebsiella, and its expression rescues a loss-of-function DeltabamA mutant. We developed an E. coli model system to measure and compare the specific activity of BamA and BamK in the assembly reaction for the critical substrate LptD, and find that BamK is as efficient as BamA in assembling the native LptDE complex. Comparative structural analysis revealed that the major distinction between BamK and BamA is in the external facing surface of the protein, and we discuss how such changes may contribute to a mechanism for resistance against infection by bacteriophage. This article is protected by copyright. All rights reserved.

KW - BAM complex

KW - BamA

KW - hypervirulence

KW - cell wall

KW - beta-barrel proteins

U2 - 10.1111/mmi.13990

DO - 10.1111/mmi.13990

M3 - Article

VL - 109

SP - 584

EP - 599

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 5

ER -