Protective immune-response of Aeromonas hydrophila phage lysate in crucian carp against direct virulent challenge with A. hydrophila-TPS.

Aeromonas hydrophila was a common opportunistic pathogen that was widely found in various aquatic environment and could cause multiple infections in humans and animals. The haemorrhagic septicemia and bacterial enteritis in fish triggered by this pathogen led to significant losses in the aquaculture industry. In this study, we aimed to develop a phage lysate vaccine by lysing the A.

Mycobacterium tuberculosis protease Rv3090 is associated with late cell apoptosis and participates in organ injuries and mycobacterial dissemination in mice.

Tuberculosis (TB) is an infectious disease caused by Mycobacterium tuberculosis (Mtb). Mtb can overcome macrophage intracellular killing and lead to persistent infections. The proteases of Mtb are critical virulence factors that participate in immune responses.

DosR Regulates the Transcription of the Arginine Biosynthesis Gene Cluster by Binding to the Regulatory Sequences in Bacille Calmette-Guerin.

l-Arginine serves as a carbon and nitrogen source and is critical for (Mtb) survival in the host. Generally, ArgR acts as a repressor regulating arginine biosynthesis by binding to the promoter of the gene cluster. In this study, we report that the dormancy regulator DosR is a novel arginine regulator binding to the promoter region of (), which regulates arginine synthesis.

Extracellular DNase MAP3916c attacks the neutrophil extracellular traps and is needed for Mycobacterium avium subsp. paratuberculosis virulence.

Extracellular DNases/nucleases are important virulence factors in many bacteria. However, no DNase/nucleases have been reported in Mycobacterium avium subsp. paratuberculosis (MAP), which is a pathogen of paratuberculosis.

Rv3091, An Extracellular Patatin-Like Phospholipase in , Prolongs Intracellular Survival of Recombinant by Mediating Phagosomal Escape.

Patatin-like phospholipases (PLPs) are important virulence factors of many pathogens. However, there are no prevailing studies regarding PLPs as a virulence factor of (Mtb). Analysis of Rv3091, a putative protein of Mtb, shows that it belongs to the PLPs family.

A unique combination of glycoside hydrolases in specifically and sequentially acts on host-derived αGal-epitope glycans.

Infections by many bacterial pathogens rely on their ability to degrade host glycans by producing glycoside hydrolases (GHs). Here, we discovered a conserved multifunctional GH, SsGalNagA, containing a unique combination of two family 32 carbohydrate-binding modules (CBM), a GH16 domain and a GH20 domain, in the zoonotic pathogen 05ZYH33. Enzymatic assays revealed that the SsCBM-GH16 domain displays -(β1,4)-galactosidase activity specifically toward the host-derived αGal epitope Gal(α1,3)Gal(β1,4)Glc(NAc)-R, whereas the SsGH20 domain has a wide spectrum of -β--acetylhexosaminidase activities, including -(β1,3)--acetylglucosaminidase activity, and employs this activity to act in tandem with SsCBM-GH16 on the αGal-epitope glycan.

Vitamin B and Vitamin C Affect DNA Methylation and Amino Acid Metabolism in BCG.

Vitamins are essential nutrients and key cofactors of enzymes that regulate cellular metabolism, and also activate the immune system. Recent studies have shown that vitamin B1 (V ) and vitamin C (Vc) can inhibit growth, but the precise mechanism is still not well understood. In the present study, we have used RNA-sequencing (RNA-seq), liquid chromatography coupled to mass spectrometry (LC-MS) and single-molecule real-time (SMRT) sequencing to analyze the transcriptional, metabolic and methylation profiles of BCG when treated with V and Vc.

Characterization and pathogenicity of extracellular serine protease MAP3292c from Mycobacterium avium subsp. paratuberculosis.

Serine protease is the virulence factor of many pathogens. However, there are no prevailing data available for serine protease as a virulence factor derived from Mycobacterium avium subsp. paratuberculosis (MAP).

Characterization of a novel Mycobacterium tuberculosis serine protease (Rv3194c) activity and pathogenicity.

Mycobacterium tuberculosis (MTB) serine proteases are important pathogen-associated virulence factors that are involved in the invasion, bacterial persistence, and degradation of host defense factors. The current study identified and characterized a novel serine protease, Rv3194c, of MTB. A heterologous Rv3194c protein, purified from Escherichia coli, possessed proteolytic activity that could hydrolyze bovine serum albumin (BSA), milk, casein, and gelatin at an optimal temperature of 40 °C and a pH of 8.

The prominent alteration in transcriptome and metabolome of Mycobacterium bovis BCG str. Tokyo 172 induced by vitamin B.

Background: Vitamin B (V) is a crucial dietary nutrient and essential cofactor for several key enzymes in the regulation of cellular and metabolic processes, and more importantly in the activation of immune system. To date, the precise role of V in Mycobacterium tuberculosis remains to be fully understood.

Results: In this study, the transcriptional and metabolic profiles of V-treated Mycobacterium.

PE17 protein from Mycobacterium tuberculosis enhances Mycobacterium smegmatis survival in macrophages and pathogenicity in mice.

The capacity of Mycobacterium tuberculosis to survive and cause disease is strongly correlated with its ability to escape multiple defense strategies in hosts. In particular, M. tuberculosis has the remarkable capacity to survive within the hostile environment of macrophages.

Extracellular Sphingomyelinase Rv0888 of Contributes to Pathological Lung Injury of in Mice Inducing Formation of Neutrophil Extracellular Traps.

is the causative agent of tuberculosis (TB), which mainly causes pulmonary injury and tubercles. Although macrophages are generally considered to harbor the main cells of , new evidence suggests that neutrophils are rapidly recruited to the infected lung. itself, or its early secreted antigenic target protein 6 (ESAT-6), can induce formation of neutrophil extracellular traps (NETs).

induces a strong Th1 response that subsequently declines in C57BL/6 mice.

is a fast-growing species of saprophytic bacteria that is widely distributed. To understand the host immune responses induced by isolated from bovine submaxillary lymph nodes, C57BL/6 mice were infected with reference strain Bacillus Calmette-Guérin (BCG) and isolated using intraperitoneal injections. Comparison of the bacterial replication and organ pathology between and BCG revealed that was more malignant than in mice.

Therapeutic effect of Pseudomonas aeruginosa phage YH30 on mink hemorrhagic pneumonia.

Hemorrhagic pneumonia caused by Pseudomonas aeruginosa remains one of the most costly infectious diseases among farmed mink and commonly leads to large economic losses during mink production. The objective of this study was to investigate the potential of using phages as a therapy against hemorrhagic pneumonia in mink. A broad-host-range phage from the Podoviridae family, YH30, was isolated using the mink-originating P.

Therapeutic effect of the YH6 phage in a murine hemorrhagic pneumonia model.

The treatment, in farmed mink, of hemorrhagic pneumonia caused by multidrug-resistant Pseudomonas aeruginosa strains has become increasingly difficult. This study investigated the potential use of phages as a therapy against hemorrhagic pneumonia caused by P. aeruginosa in a murine hemorrhagic pneumonia model.

Salmonella Typhimurium strain expressing OprF-OprI protects mice against fatal infection by Pseudomonas aeruginosa.

Pseudomonas aeruginosa poses a major threat to human health and to the mink industry. Thus, development of vaccines that elicit robust humoral and cellular immunity against P. aeruginosa is greatly needed.

Mannose-modified chitosan microspheres enhance OprF-OprI-mediated protection of mice against Pseudomonas aeruginosa infection via induction of mucosal immunity.

Pseudomonas aeruginosa is an opportunistic pathogen that localizes to and colonizes mucosal tissue. Thus, vaccines that elicit a strong mucosal response against P. aeruginosa should be superior to other vaccination strategies.

Structural and biochemical characterization reveals LysGH15 as an unprecedented "EF-hand-like" calcium-binding phage lysin.

The lysin LysGH15, which is derived from the staphylococcal phage GH15, demonstrates a wide lytic spectrum and strong lytic activity against methicillin-resistant Staphylococcus aureus (MRSA). Here, we find that the lytic activity of the full-length LysGH15 and its CHAP domain is dependent on calcium ions. To elucidate the molecular mechanism, the structures of three individual domains of LysGH15 were determined.