Proteomic analysis of microbial induced redox-dependent intestinal signaling
Jason D. Matthews,
April R. Reedy,
Huixia Wu,
Benjamin H. Hinrichs,
Trevor M. Darby,
Caroline Addis,
Brian S. Robinson,
Young-Mi Go,
Dean P. Jones,
Rheinallt M. Jones,
Andrew S. Neish
Affiliations
Jason D. Matthews
Department of Pathology, Emory University School of Medicine, Atlanta, GA, USA
April R. Reedy
Department of Pathology, Emory University School of Medicine, Atlanta, GA, USA
Huixia Wu
Department of Pathology, Emory University School of Medicine, Atlanta, GA, USA
Benjamin H. Hinrichs
Department of Pathology, Emory University School of Medicine, Atlanta, GA, USA
Trevor M. Darby
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, USA
Caroline Addis
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, USA
Brian S. Robinson
Department of Pathology, Emory University School of Medicine, Atlanta, GA, USA
Young-Mi Go
Department of Medicine, Emory University School of Medicine, Atlanta, GA, USA
Dean P. Jones
Department of Medicine, Emory University School of Medicine, Atlanta, GA, USA
Rheinallt M. Jones
Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, USA
Andrew S. Neish
Department of Pathology, Emory University School of Medicine, Atlanta, GA, USA; Correspondence to: Department of Pathology, Emory University School of Medicine, Room 105A, Whitehead Bldg., 615 Michael Street, Atlanta, GA 30322, USA.
Intestinal homeostasis is regulated in-part by reactive oxygen species (ROS) that are generated in the colonic mucosa following contact with certain lactobacilli. Mechanistically, ROS can modulate protein function through the oxidation of cysteine residues within proteins. Recent advances in cysteine labeling by the Isotope Coded Affinity Tags (ICATs) technique has facilitated the identification of cysteine thiol modifications in response to stimuli. Here, we used ICATs to map the redox protein network oxidized upon initial contact of the colonic mucosa with Lactobacillus rhamnosus GG (LGG). We detected significant LGG-specific redox changes in over 450 proteins, many of which are implicated to function in cellular processes such as endosomal trafficking, epithelial cell junctions, barrier integrity, and cytoskeleton maintenance and formation. We particularly noted the LGG-specific oxidation of Rac1, which is a pleiotropic regulator of many cellular processes. Together, these data reveal new insights into lactobacilli-induced and redox-dependent networks involved in intestinal homeostasis.
