Invasion and Dissemination of Yersinia enterocolitica in the Mouse Infection Model

Abstract

Yersinia enterocolitica is one of the most common causes of food borne gastrointestinal disease. After oral uptake yersiniae replicate in the small intestine, invade Peyer's patches of the distal ileum and disseminate to spleen and liver. In these tissues and organs yersiniae replicate extracellularly and form exclusively monoclonal microabscesses. Only very few yersiniae invade Peyer's patches and establish just a very few monoclonal microabscesses. This is due to both Yersinia and host specific factors.

Different Bacterial Pathogens, Different Strategies, Yet the Aim Is the Same: Evasion of Intestinal Dendritic Cell Recognition

“…Yersinia enterocolitica is a Gram-negative bacterium that causes foodborne acute and chronic gastrointestinal diseases (55). Ingested Y. enterocolitica are taken up by M cells, colonize Peyer's patches, and disseminate to liver and spleen (56). Despite its predominantly extracellular lifestyle, the bacteria have a TTSS, allowing them to inject a number of effector proteins, including Yersinia outer proteins (Yops) into host cells.…”

Cytotoxic Necrotizing Factor-Y Boosts Yersinia Effector Translocation by Activating Rac Protein

“…After oral ingestion, the enteropathogenic Yersinia spp. reach the distal small intestine, from where a subset invades and crosses the intestinal mucosa mainly via M-cells (3). Once the yersiniae have reached the mucosa-associated lymphatic tissue, they subvert immune cell responses such as phagocytosis and cytokine production and proliferate extracellularly (4,5).…”

“…Most Rho GTP-binding proteins cycle between an inactive GDP-bound and an active GTPbound state. The cycling is tightly controlled by three sets of regulatory proteins: guanine nucleotide exchange factors, which catalyze the exchange of bound GDP for GTP; GTPase-activating proteins (GAPs), 3 which strongly accelerate the intrinsic GTPase activity; and guanine nucleotide dissociation inhibitors, which extract the GDP-bound form from membranes and keep it in the cytosol (30,31). The multidomain YopO/YpkA comprises a G-actin-activated serine/threonine kinase module and a module that structurally and functionally mimics a guanine nucleotide dissociation inhibitor, which was reported to bind and inhibit Rac1 (32)(33)(34)(35).…”

Mononuclear phagocytes contribute to intestinal invasion and dissemination of Yersinia enterocolitica

“…The follicle-associated epithelium contains high number of M cells, which actively internalize Ags by endocytosis, phagocytosis or macropinocytosis and transfer them to underlying follicle to induce an appropriate immune response (Schulz and Pabst, 2012). It is well known that Ye invades through M cells by binding to ␤1-integrins, thereby mediating internalization and colonization of PPs (Autenrieth and Firsching, 1996;Clark et al, 1998;Trülzsch et al, 2007). Thereafter, Ye disseminates via lymph and/or blood to MLN, spleen and liver (Carter, 1975).…”