Author Correction:Single human B cell-derived monoclonal anti-Candida antibodies enhance phagocytosis and protect against disseminated candidiasis

We thank the BBSRC, SULSA BioSKAPE and Pfizer Inc. for funding for a studentship for F.M.R. and the Wellcome Trust (086827, 075470, 099215, 099197 and 101873) and a Wellcome Trust ISSF award (105625), MRC CiC (MC_PC_14114) and MRC Centre for Medical Mycology and University of Aberdeen for funding and a Wellcome Trust Strategic Award (097377) and a Wellcome Trust grant 099197MA to T.F. and FCT Investigator IF/00033/2012 and PTDC/QUI-QUI/112537/2009 to A.S.P. We thank Ian Broadbent, Angus McDonald and Ron Gladue for constructive discussions; Chris Boston and Amanda Fitzgerald for advice on antibody expression and purification; Ed Lavallie and Wayne Stochaj for design and expression of the recombinant Hyr1; Louise Walker for high-pressure freezing of samples for TEM analysis; Jeanette Wagener for endotoxin testing of mAbs for in vivo experiments; Yan Liu of the Glycosciences laboratory for insight in the analysis with N-glycan array; Rebecca Hall and Mark Gresnigt for providing fungal strains; Andrew Limper and Theodore J. Kottom for providing Pneumocystis infected lung tissue extracts; David Williams for C. albicans mannoprotein; Christopher Thornton for A. fumigatus mannoprotein; Katie J. Doores for mAb PGT 128; and Gordon Brown for the murine Fc-Dectin-1. We are grateful to Lucinda Wight, Debbie Wilkinson and Kevin MacKenzie in the Microscopy and Histology Core Facility (Aberdeen University) and Raif Yuecel in the Iain Fraser Cytometry Centre (Aberdeen University) for their expert help with microscopy and cytometry experiments. We are also grateful to the staff at the University of Aberdeen Medical Research Facility for assistance with in vivo experiments and members of the Glycosciences Laboratory for their support of the Carbohydrate Microarray Facility. 18 January 2019 - Author Correction: Single human B cell-derived monoclonal anti-Candida antibodies enhance phagocytosis and protect against disseminated candidiasis F. M. Rudkin, I. Raziunaite, H. Workman, S. Essono, R. Belmonte, D. M. MacCallum, E. M. Johnson, L. Silva, A. S. Palma, T. Feizi, A. Jensen, L. P. Erwig & N. A. R. Gow Nature Communicationsvolume 10, Article number: 394 (2019)Peer reviewedPublisher PD

Ecto-ADP-ribosyltransferase ARTC2.1 functionally modulates FcγR1 and FcγR2B on murine microglia

Mammalian ecto-ADP-ribosyltransferases (ecto-ARTs or also ARTCs) catalyze the ADP-ribosylation of cell surface proteins using extracellular nicotinamide adenine dinucleotide (NAD+) as substrate. By this post-translational protein modification, ecto-ARTs modulate the function of various target proteins. A functional role of ARTC2 has been demonstrated for peripheral immune cells such as T cells and macrophages. Yet, little is known about the role of ecto-ARTs in the central nervous system and on microglia. Here, we identified ARTC2.1 as the major ecto-ART expressed on murine microglia. ARTC2.1 expression was strongly upregulated on microglia upon co-stimulation with LPS and an ERK1/2 inhibitor or upon IFNβ stimulation. We identified several target proteins modified by ARTC2.1 on microglia with a recently developed mass spectrometry approach, including two receptors for immunoglobulin G (IgG), FcγR1 and FcγR2B. Both proteins were verified as targets of ARTC2.1 in vitro using a radiolabeling assay with 32P-NAD+ as substrate. Moreover, ADP-ribosylation of both targets strongly inhibited their capacity to bind IgG. In concordance, ARTC2.1 induction in WT microglia and subsequent cell surface ADP-ribosylation significantly reduced the phagocytosis of IgG-coated latex beads, which was unimpaired in NAD+/DTT treated microglia from ARTC2.1-/- mice. Hence, induction of ARTC2.1 expression under inflammatory conditions, and subsequent ADP-ribosylation of cell surface target proteins could represent a hitherto unnoticed mechanism to regulate the immune response of murine microglia