CpaA Is a Glycan-Specific Adamalysin-like Protease Secreted by Acinetobacter baumannii That Inactivates Coagulation Factor XII

Abstract

Ventilator-associated pneumonia and catheter-related bacteremia are the most common and severe infections caused byAcinetobacter baumannii. Besides the capsule, lipopolysaccharides, and the outer membrane porin OmpA, little is known about the contribution of secreted proteins toA. baumanniisurvivalin vivo. Here we focus on CpaA, a potentially recently acquired virulence factor that inhibits blood coagulationin vitro. We identify coagulation factor XII as a target of CpaA, map the cleavage sites, and show that glycosylation is a prerequisite for CpaA-mediated inactivation of factor XII. We propose adding CpaA to a small, but growing list of bacterial proteases that are specific for highly glycosylated components of the host defense system.

Document Details

Document Type
Pub Defense Publication
Publication Date
Dec 21, 2018
Source ID
10.1128/mbio.01606-18

Entities

People

  • Alban Deroux
  • Andrew Yee
  • Ayush Kumar
  • Daniel A. Lawrence
  • David Ginsburg
  • Harry L. T. Mobley
  • Maria Sandkvist
  • Mark Warnock
  • Sara Smith
  • Ursula Waack
  • Zachary Huttinger

Organizations

  • Centre hospitalier universitaire de Grenoble
  • Howard Hughes Medical Institute
  • Michigan Medicine
  • National Heart, Lung, and Blood Institute
  • National Institute of Allergy and Infectious Diseases
  • United States Department of Defense
  • University of Manitoba
  • University of Michigan

Tags

Fields of Study

  • Biology

Readers

  • Mathematics or Statistics
  • Microbial Pathology
  • Molecular Genetics