PplD is a de-N-acetylase of the cell wall linkage unit of streptococcal rhamnopolysaccharides

Jeffrey S. Rush, Prakash Parajuli, Alessandro Ruda, Jian Li, Amol Arunrao Pohane, Svetlana Zamakhaeva, Mohammad M. Rahman, Jennifer C. Chang, Artemis Gogos, Cameron W. Kenner, Gérard Lambeau, Michael J. Federle, Konstantin V. Korotkov, Göran Widmalm and Natalia Korotkova ()
Additional contact information
Jeffrey S. Rush: University of Kentucky
Prakash Parajuli: University of Kentucky
Alessandro Ruda: Stockholm University
Jian Li: University of Kentucky
Amol Arunrao Pohane: University of Kentucky
Svetlana Zamakhaeva: University of Kentucky
Mohammad M. Rahman: University of Kentucky
Jennifer C. Chang: University of Illinois at Chicago
Artemis Gogos: University of Illinois at Chicago
Cameron W. Kenner: University of Kentucky
Gérard Lambeau: Université Côte d’Azur, Centre National de la Recherche Scientifique, Institut de Pharmacologie Moléculaire et Cellulaire
Michael J. Federle: University of Illinois at Chicago
Konstantin V. Korotkov: University of Kentucky
Göran Widmalm: Stockholm University
Natalia Korotkova: University of Kentucky

Nature Communications, 2022, vol. 13, issue 1, 1-16

Abstract: Abstract The cell wall of the human bacterial pathogen Group A Streptococcus (GAS) consists of peptidoglycan decorated with the Lancefield group A carbohydrate (GAC). GAC is a promising target for the development of GAS vaccines. In this study, employing chemical, compositional, and NMR methods, we show that GAC is attached to peptidoglycan via glucosamine 1-phosphate. This structural feature makes the GAC-peptidoglycan linkage highly sensitive to cleavage by nitrous acid and resistant to mild acid conditions. Using this characteristic of the GAS cell wall, we identify PplD as a protein required for deacetylation of linkage N-acetylglucosamine (GlcNAc). X-ray structural analysis indicates that PplD performs catalysis via a modified acid/base mechanism. Genetic surveys in silico together with functional analysis indicate that PplD homologs deacetylate the polysaccharide linkage in many streptococcal species. We further demonstrate that introduction of positive charges to the cell wall by GlcNAc deacetylation protects GAS against host cationic antimicrobial proteins.

Date: 2022
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DOI: 10.1038/s41467-022-28257-0

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