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

Rush, Jeffrey S.; Parajuli, Prakash; Ruda, Alessandro; Li, Jian; Pohane, Amol Arunrao; Zamakhaeva, Svetlana; Rahman, Mohammad M.; Chang, Jennifer C.; Gogos, Artemis; Kenner, Cameron W.; Lambeau, Gérard; Federle, Michael J.; Korotkov, Konstantin V.; Widmalm, Göran; Korotkova, Natalia

doi:10.1038/s41467-022-28257-0

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

Journal Article · 01 February 2022 · Nature Communications

DOI: https://doi.org/10.1038/s41467-022-28257-0 · OSTI ID:1903964

Rush, Jeffrey S. ^[1];

^[2];

^[3]; Li, Jian ^[2];

^[2]; Zamakhaeva, Svetlana ^[2]; Rahman, Mohammad M. ^[2];

^[4];

^[4]; Kenner, Cameron W. ^[2];

^[5];

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^[2];

^[3];

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University of Kentucky, Lexington, KY (United States); OSTI
University of Kentucky, Lexington, KY (United States)
Stockholm University (Sweden)
University of Illinois, Chicago, IL (United States)
Universite Cote d'Azur, Nice (France)

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.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL); University of Kentucky, Lexington, KY (United States)

Sponsoring Organization:: Knut and Alice Wallenberg Foundation; National Institutes of Health (NIH); Swedish Research Council; USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); University of Gothenburg

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1903964

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 13; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
bacterial structural biology
polysaccharides
solution-state NMR
x-ray crystallography

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

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