Disease relevance of yopN

• The yopN gene was shown to encode a protein (formerly also designated Yop4b) which is surface-located when Yersinia is grown at 37 degrees C. yopN was found to be part of an operon that is induced during the low-calcium response [1].
• Leakage of the reporters into the macrophage culture supernatant during the bacterial infection increased strongly when YopN was missing, showing that YopN is involved in the control of delivery of YopM inside eukaryotic cells [2].

High impact information on yopN

• Yop secretion is triggered by contact with eukaryotic cells and controlled by proteins of the virulon including YopN, TyeA, and LcrG, which are thought to form a plug complex closing the bacterial secretion channel [3].
• YopN itself was not delivered into the macrophages [2].
• Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y.enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus [2].
• The predicted amino acid sequence of InvE showed significant homology to the Yersinia outer membrane protein YopN (LcrE) [4].
• The role of these proteins was investigated in the translocation of Elk-tagged YopE (YopE129-Elk) and YopN (YopN293-Elk) into HeLa cells [5].

Biological context of yopN

• A hybrid plasmid containing the yopN gene under the control of the tac promoter fully restored the wild-type phenotype of the yopN mutant [1].
• The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis [1].
• The modeled assembly features the secretion signaling elements of YopN at one end of an elongated structure and the secretion regulating TyeA binding site at the other [6].
• The type III secretion signal of Yersinia enterocolitica YopN was mapped using a gene fusion approach. yopN codons 1 to 12 were identified as critical for signal function [7].
• The sequence of lcrE locus revealed six tightly packed open reading frames (ORFs), one of which was identified as the structural gene, lcrE, of the 32.9-kilodalton outer membrane protein LcrE (formerly known as Yop4b or YopN) [8].

Anatomical context of yopN

• CopN is homologous to the secreted protein YopN of Yersinia sp., and analysis of monolayers 20 h after infection via indirect immunofluorescence showed specific labelling of inclusion membranes when probed with CopN-specific antibodies but not with Scc1-specific antibodies [9].
• In an in vitro assay, the translocation system causes the lysis of erythrocytes infected with wild-type (wt) P. aeruginosa. wt Y. enterocolitica is not hemolytic, but a multiknockout mutant deprived of all the effectors and of YopN ( Delta HOPEMN) is hemolytic [10].

Associations of yopN with chemical compounds

• As crystallization efforts remained fruitless, even after the proteolysis-guided engineering of a truncated YopN polypeptide, reductive methylation of lysine residues was employed to alter the surface properties of the complex [11].

Analytical, diagnostic and therapeutic context of yopN

• Protease protection, cell fractionation, and affinity purification experiments suggest that TyeA is located intracellularly and binds to YopN or YopD [12].

References