Journal article
The Glycoprotease CpaA Secreted by Medically Relevant Acinetobacter Species Targets Multiple O-Linked Host Glycoproteins
MF Haurat, NE Scott, G Di Venanzio, J Lopez, B Pluvinage, AB Boraston, MJ Ferracane, MF Feldman
mBio | AMER SOC MICROBIOLOGY | Published : 2020
Abstract
Glycans decorate proteins and affect their biological function, including protection against proteolytic degradation. However, pathogenic, and commensal bacteria have evolved specific glycoproteases that overcome the steric impediment posed by carbohydrates, cleaving glycoproteins precisely at their glycosylation site(s). Medically relevant Acinetobacter strains employ their type II secretion system (T2SS) to secrete the glycoprotease CpaA, which contributes to virulence. Previously, CpaA was shown to cleave two O-linked glycoproteins, factors V and XII, leading to reduced blood coagulation. In this work, we show that CpaA cleaves a broader range of O-linked human glycoproteins, including se..
View full abstractGrants
Awarded by Washington University School of Medicine in St. Louis
Funding Acknowledgements
[ "Flow cytometry experiments were performed at the Flow Cytometry & Fluorescence Activated Cell Sorting Core (Department of Pathology & Immunology, Washington University School of Medicine in St. Louis). Protein-Glycan Interaction Resource of the CFG (supporting grant R24 GM098791), and the National Center for Functional Glycomics (NCFG) at Beth Israel Deaconess Medical Center, Harvard Medical School (supporting grant P41 GM103694). We thank the Melbourne Mass Spectrometry and Proteomics Facility of The Bio21 Molecular Science and Biotechnology Institute for access to MS instrumentation. We thank Paula Magnelli (New England Biolabs) for generously providing us Etanercept and Abatacept. We thank the members of the Feldman lab for critical reading of the manuscript.", "This work was supported by a National Health and Medical Research Council of Australia (NHMRC) project grant awarded to N.E.S. (APP1100164) and a Canadian Institutes of Health Research project grant to A.B.B. (PJT 159786). This work was also supported by grants from the National Institute of Allergy and Infectious Diseases grant R01AI144120 awarded to M.F.F." ]