Microneme Protein 3 Inhibits Apoptosis of the Chicken Duodenal Epithelial Cell by Targeting the Casitas B-Lineage Lymphoma Protein.

() causes coccidiosis in poultry which persists as economic pain worldwide. Most damage to the intestinal mucosa results from apoptosis of the infected intestinal epithelial cells. The Microneme protein 3 (MIC3) protein is a key virulence factor in some parasites involved in host cell apoptosis inhibition.

Regulated delayed attenuation improves vaccine efficacy in preventing infection from avian pathogenic Escherichia coli O and Salmonella typhimurium.

Avian pathogenic Escherichia coli (APEC) O and Salmonella typhimurium (S. Typhimurium) are two leading bacterial pathogens that cause significant economic loss in the poultry industry. O-antigen is an important immunogen of these two bacteria to induce host protective immune responses during infection.

Mycobacterial PPE13 activates inflammasome by interacting with the NATCH and LRR domains of NLRP3.

Pathogenic mycobacteria, such as Mycobacterium tuberculosis, Mycobacterium bovis, and Mycobacterium marinum, can trigger NLRP3 inflammasome activation leading to maturation and secretion of interleukin 1β (IL-1β). However, the mycobacterial factors involved in the activation of NLRP3 inflammasome are not fully understood. Here, we identified that the PPE family protein PPE13 was responsible for the induction of IL-1β secretion in a NLRP3 inflammasome-dependent manner.

Listeriolysin O Pore-Forming Activity Is Required for ERK1/2 Phosphorylation During Infection.

Listeriolysin O (LLO) is a cholesterol-dependent cytolysin that mediates escape of from phagosomes and enables the bacteria to grow within the host. LLO is a versatile tool allowing to trigger several cellular responses. In this study, rapid phosphorylation of ERK1/2 on Caco-2 cells caused by infection was demonstrated to be highly dependent on LLO activity.

An M29 Aminopeptidase from Contributes to In Vitro Bacterial Growth but not to Intracellular Infection.

Aminopeptidases that catalyze the removal of N-terminal residues from polypeptides or proteins are crucial for physiological processes. Here, we explore the biological functions of an M29 family aminopeptidase II from (LmAmpII). We show that LmAmpII contains a conserved catalytic motif (EEHYHD) that is essential for its enzymatic activity and LmAmpII has a substrate preference for arginine and leucine.

Fine mapping of a linear epitope on EDIII of Japanese encephalitis virus using a novel neutralizing monoclonal antibody.

The domain III (EDIII) of the envelope protein of Japanese encephalitis virus (JEV) is proposed to play an essential role in JEV replication and infection; it is involved in binding to host receptors and contains specific epitopes that elicit neutralizing antibodies. However, most previous studies have not provided detailed molecular information about the functional epitopes on JEV EDIII protein. In this study, we described a monoclonal antibody (mAb 2B4) we produced and characterized by IFA, PRNT, ELISA and Western blot analyses.