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Correction: The N-glycan Glycoprotein Deglycosylation Complex (Gpd) from Capnocytophaga canimorsus Deglycosylates Human IgG ((2015), 11, 12)

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RESEARCH OUTPUTS / RÉSULTATS DE RECHERCHE

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Correction

Renzi, Francesco; Manfredi, Pablo; Mally, Manuela; Moes, Suzette; Jenö, Paul; Cornelis, Guy

R.

Published in:

Plos Pathogens

DOI:

10.1371/journal.ppat.1005352

Publication date:

2015

Document Version

Publisher's PDF, also known as Version of record

Link to publication

Citation for pulished version (HARVARD):

Renzi, F, Manfredi, P, Mally, M, Moes, S, Jenö, P & Cornelis, GR 2015, 'Correction: The N-glycan Glycoprotein

Deglycosylation Complex (Gpd) from Capnocytophaga canimorsus Deglycosylates Human IgG ((2015), 11, 12)',

Plos Pathogens, vol. 11, no. 12, e1005352. https://doi.org/10.1371/journal.ppat.1005352

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CORRECTION

Correction: The N-glycan Glycoprotein

Deglycosylation Complex (Gpd) from

Capnocytophaga canimorsus Deglycosylates

Human IgG

Francesco Renzi, Pablo Manfredi, Manuela Mally, Suzette Moes, Paul Jenö, Guy

R. Cornelis

The authors would like to correct

Fig 6B

. The blot depicted in

Fig 6B

contains two errors: 1)

the blot has been assembled by cropping and moving lanes from different parts of a same

mem-brane without indication of this manipulation in the figure and in the legend; 2) the blot

dis-plays duplicated data in two lanes. These errors occurred during assembly of the final figure.

The authors have corrected

Fig 6B

replacing the duplicated lanes with the correct ones and

have boxed the lanes that were cropped and moved from the same or different blots.

The authors confirm that these changes do not alter their findings. The authors have

pro-vided raw, uncropped blots as Supporting Information.

PLOS Pathogens | DOI:10.1371/journal.ppat.1005352 December 15, 2015 1 / 3 OPEN ACCESS

Citation: Renzi F, Manfredi P, Mally M, Moes S, Jenö P, Cornelis GR (2015) Correction: The N-glycan Glycoprotein Deglycosylation Complex (Gpd) from Capnocytophaga canimorsus Deglycosylates Human IgG. PLoS Pathog 11(12): e1005352. doi:10.1371/ journal.ppat.1005352

Published: December 15, 2015

Copyright: © 2015 Renzi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 6. Lipid modification of GpdD and GpdG is essential for their activity. (A) Number of divisions after 23 h growth on HEK293 cells ofΔgpdG bacteria complemented with gpdGC21Gand ofΔgpdD bacteria

complemented with gpdDC17G. (B) Fetuin glycosylation state of samples incubated for 2 hours in the

presence of the different strains, determined by staining with SNA. (C) Same as B analyzed by western blot

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Supporting Information

S1 Fig. Uncropped blots.

Original unmodified blots used for the assembly of

Fig 6B

. The lanes

used in

Fig 6B

are identified and labeled.

(TIF)

Reference

1. Renzi F, Manfredi P, Mally M, Moes S, Jenö P, Cornelis GR (2011) The N-glycan Glycoprotein Degly-cosylation Complex (Gpd) from Capnocytophaga canimorsus Deglycosylates Human IgG. PLoS Pathog 7(6): e1002118. doi:10.1371/journal.ppat.1002118PMID:21738475

with anti-fetuin antibodies. The boxes indicate lanes that have been cropped and moved either from a same or a different blot.

doi:10.1371/journal.ppat.1005352.g001

Figure

Fig 6. Lipid modification of GpdD and GpdG is essential for their activity. (A) Number of divisions after 23 h growth on HEK293 cells of Δ gpdG bacteria complemented with gpdG C21G and of Δ gpdD bacteria complemented with gpdD C17G

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