Correction: Corrigendum: Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism

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Nature 517, 165–169 (2015); doi:10.1038/nature13995

In this Article focusing on the selfish metabolism of yeast mannan by Bacteroidetes, we also described a polysaccharide utilization locus (PUL) responsible for the degradation of high mannose mammalian N-glycan (HMNG) but omitted to cite two relevant papers1,2, for which we apologise. Both studies describe a model for the degradation of complex biantennary N-glycans by Bacteroidetes in which the degradative enzymes are encoded by PULs. These studies1,2 provide examples of how PULs can orchestrate N-glycan metabolism in addition to the HMNG PUL we describe in this Article. In all three papers it is proposed that N-glycan depolymerization occurs primarily in the periplasm.

References

  1. 1

    Renzi, F. et al. The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG. PLoS Pathog. 7, e1002118 (2011)

  2. 2

    Nihira, T. et al. Discovery of β-1,4-d-mannosyl-N-acetyl-d-glucosamine phosphorylase involved in the metabolism of N-glycans. J. Biol. Chem. 288, 27366–27374 (2013)

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The online version of the original article can be found at 10.1038/nature13995

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