Uncovering a novel molecular mechanism for scavenging sialic acids in bacteria

J Biol Chem. 2020 Oct 2;295(40):13724-13736. doi: 10.1074/jbc.RA120.014454. Epub 2020 Jul 15.

Abstract

The human gut symbiont Ruminococcus gnavus scavenges host-derived N-acetylneuraminic acid (Neu5Ac) from mucins by converting it to 2,7-anhydro-Neu5Ac. We previously showed that 2,7-anhydro-Neu5Ac is transported into R. gnavus ATCC 29149 before being converted back to Neu5Ac for further metabolic processing. However, the molecular mechanism leading to the conversion of 2,7-anhydro-Neu5Ac to Neu5Ac remained elusive. Using 1D and 2D NMR, we elucidated the multistep enzymatic mechanism of the oxidoreductase (RgNanOx) that leads to the reversible conversion of 2,7-anhydro-Neu5Ac to Neu5Ac through formation of a 4-keto-2-deoxy-2,3-dehydro-N-acetylneuraminic acid intermediate and NAD+ regeneration. The crystal structure of RgNanOx in complex with the NAD+ cofactor showed a protein dimer with a Rossman fold. Guided by the RgNanOx structure, we identified catalytic residues by site-directed mutagenesis. Bioinformatics analyses revealed the presence of RgNanOx homologues across Gram-negative and Gram-positive bacterial species and co-occurrence with sialic acid transporters. We showed by electrospray ionization spray MS that the Escherichia coli homologue YjhC displayed activity against 2,7-anhydro-Neu5Ac and that E. coli could catabolize 2,7-anhydro-Neu5Ac. Differential scanning fluorimetry analyses confirmed the binding of YjhC to the substrates 2,7-anhydro-Neu5Ac and Neu5Ac, as well as to co-factors NAD and NADH. Finally, using E. coli mutants and complementation growth assays, we demonstrated that 2,7-anhydro-Neu5Ac catabolism in E. coli depended on YjhC and on the predicted sialic acid transporter YjhB. These results revealed the molecular mechanisms of 2,7-anhydro-Neu5Ac catabolism across bacterial species and a novel sialic acid transport and catabolism pathway in E. coli.

Keywords: 2,7-anhydro-Neu5AC; 2,7-anhydro-Neu5Ac; Escherichia coli; Escherichia coli (E. coli); Ruminococcus gnavus; STD NMR; gut microbiota; gut symbiosis; microbiology; mucin glycosylation; nuclear magnetic resonance (NMR); oxidation-reduction (redox); oxidoreductase; sialic acid; sialic acid transporters; symbiosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Clostridiales / enzymology*
  • Clostridiales / genetics
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Genetic Complementation Test
  • Humans
  • Mucins / chemistry
  • Mucins / metabolism
  • N-Acetylneuraminic Acid / chemistry*
  • N-Acetylneuraminic Acid / genetics
  • N-Acetylneuraminic Acid / metabolism
  • Oxidoreductases / chemistry*
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism

Substances

  • Bacterial Proteins
  • Mucins
  • Oxidoreductases
  • N-Acetylneuraminic Acid

Supplementary concepts

  • Ruminococcus gnavus

Associated data

  • PDB/5UI9