A lysozyme with altered substrate specificity facilitates prey cell exit by the periplasmic predator Bdellovibrio bacteriovorus

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A lysozyme with altered substrate specificity facilitates prey cell exit by the periplasmic predator Bdellovibrio bacteriovorus. / Harding, Christopher J.; Huwiler, Simona G.; Somers, Hannah; Lambert, Carey; Ray, Luke J.; Till, Rob; Taylor, Georgina; Moynihan, Patrick J.; Sockett, R. Elizabeth; Lovering, Andrew L.

In: Nature Communications, Vol. 11, No. 1, 4817 , 23.09.2020.

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Harding, Christopher J. ; Huwiler, Simona G. ; Somers, Hannah ; Lambert, Carey ; Ray, Luke J. ; Till, Rob ; Taylor, Georgina ; Moynihan, Patrick J. ; Sockett, R. Elizabeth ; Lovering, Andrew L. / A lysozyme with altered substrate specificity facilitates prey cell exit by the periplasmic predator Bdellovibrio bacteriovorus. In: Nature Communications. 2020 ; Vol. 11, No. 1.

Bibtex

@article{6d86d5721e8044d4870c544eab547c76,
title = "A lysozyme with altered substrate specificity facilitates prey cell exit by the periplasmic predator Bdellovibrio bacteriovorus",
abstract = "Lysozymes are among the best-characterized enzymes, acting upon the cell wall substrate peptidoglycan. Here, examining the invasive bacterial periplasmic predator Bdellovibrio bacteriovorus, we report a diversified lysozyme, DslA, which acts, unusually, upon (GlcNAc-) deacetylated peptidoglycan. B. bacteriovorus are known to deacetylate the peptidoglycan of the prey bacterium, generating an important chemical difference between prey and self walls and implying usage of a putative deacetyl-specific “exit enzyme”. DslA performs this role, and ΔDslA strains exhibit a delay in leaving from prey. The structure of DslA reveals a modified lysozyme superfamily fold, with several adaptations. Biochemical assays confirm DslA specificity for deacetylated cell wall, and usage of two glutamate residues for catalysis. Exogenous DslA, added ex vivo, is able to prematurely liberate B. bacteriovorus from prey, part-way through the predatory lifecycle. We define a mechanism for specificity that invokes steric selection, and use the resultant motif to identify wider DslA homologues.",
keywords = "Bacterial Proteins/genetics, Bdellovibrio bacteriovorus/enzymology, Cell Wall, Escherichia coli, Gene Expression Regulation, Bacterial, Models, Molecular, Muramidase/chemistry, Mutation, Peptidoglycan/metabolism, Periplasm/metabolism, Phenotype, Protein Conformation, Substrate Specificity",
author = "Harding, {Christopher J.} and Huwiler, {Simona G.} and Hannah Somers and Carey Lambert and Ray, {Luke J.} and Rob Till and Georgina Taylor and Moynihan, {Patrick J.} and Sockett, {R. Elizabeth} and Lovering, {Andrew L.}",
year = "2020",
month = sep,
day = "23",
doi = "10.1038/s41467-020-18139-8",
language = "English",
volume = "11",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Springer",
number = "1",

}

RIS

TY - JOUR

T1 - A lysozyme with altered substrate specificity facilitates prey cell exit by the periplasmic predator Bdellovibrio bacteriovorus

AU - Harding, Christopher J.

AU - Huwiler, Simona G.

AU - Somers, Hannah

AU - Lambert, Carey

AU - Ray, Luke J.

AU - Till, Rob

AU - Taylor, Georgina

AU - Moynihan, Patrick J.

AU - Sockett, R. Elizabeth

AU - Lovering, Andrew L.

PY - 2020/9/23

Y1 - 2020/9/23

N2 - Lysozymes are among the best-characterized enzymes, acting upon the cell wall substrate peptidoglycan. Here, examining the invasive bacterial periplasmic predator Bdellovibrio bacteriovorus, we report a diversified lysozyme, DslA, which acts, unusually, upon (GlcNAc-) deacetylated peptidoglycan. B. bacteriovorus are known to deacetylate the peptidoglycan of the prey bacterium, generating an important chemical difference between prey and self walls and implying usage of a putative deacetyl-specific “exit enzyme”. DslA performs this role, and ΔDslA strains exhibit a delay in leaving from prey. The structure of DslA reveals a modified lysozyme superfamily fold, with several adaptations. Biochemical assays confirm DslA specificity for deacetylated cell wall, and usage of two glutamate residues for catalysis. Exogenous DslA, added ex vivo, is able to prematurely liberate B. bacteriovorus from prey, part-way through the predatory lifecycle. We define a mechanism for specificity that invokes steric selection, and use the resultant motif to identify wider DslA homologues.

AB - Lysozymes are among the best-characterized enzymes, acting upon the cell wall substrate peptidoglycan. Here, examining the invasive bacterial periplasmic predator Bdellovibrio bacteriovorus, we report a diversified lysozyme, DslA, which acts, unusually, upon (GlcNAc-) deacetylated peptidoglycan. B. bacteriovorus are known to deacetylate the peptidoglycan of the prey bacterium, generating an important chemical difference between prey and self walls and implying usage of a putative deacetyl-specific “exit enzyme”. DslA performs this role, and ΔDslA strains exhibit a delay in leaving from prey. The structure of DslA reveals a modified lysozyme superfamily fold, with several adaptations. Biochemical assays confirm DslA specificity for deacetylated cell wall, and usage of two glutamate residues for catalysis. Exogenous DslA, added ex vivo, is able to prematurely liberate B. bacteriovorus from prey, part-way through the predatory lifecycle. We define a mechanism for specificity that invokes steric selection, and use the resultant motif to identify wider DslA homologues.

KW - Bacterial Proteins/genetics

KW - Bdellovibrio bacteriovorus/enzymology

KW - Cell Wall

KW - Escherichia coli

KW - Gene Expression Regulation, Bacterial

KW - Models, Molecular

KW - Muramidase/chemistry

KW - Mutation

KW - Peptidoglycan/metabolism

KW - Periplasm/metabolism

KW - Phenotype

KW - Protein Conformation

KW - Substrate Specificity

UR - http://www.scopus.com/inward/record.url?scp=85091419117&partnerID=8YFLogxK

U2 - 10.1038/s41467-020-18139-8

DO - 10.1038/s41467-020-18139-8

M3 - Article

C2 - 32968056

VL - 11

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 4817

ER -