Francisella tularensis LVS surface and membrane proteins as targets of effective post-exposure immunization for tularemia.

Francisella tularensis causes disease (tularemia) in a large number of mammals, including man. We previously demonstrated enhanced efficacy of conventional antibiotic therapy for tularemia by postexposure passive transfer of immune sera developed against a F. tularensis LVS membrane protein fraction (MPF).

Correlates of immune protection following cutaneous immunization with an attenuated Burkholderia pseudomallei vaccine.

Infections with the Gram-negative bacterium Burkholderia pseudomallei (melioidosis) are associated with high mortality, and there is currently no approved vaccine to prevent the development of melioidosis in humans. Infected patients also do not develop protective immunity to reinfection, and some individuals will develop chronic, subclinical infections with B. pseudomallei.

Interleukin-17 protects against the Francisella tularensis live vaccine strain but not against a virulent F. tularensis type A strain.

Francisella tularensis is a highly infectious intracellular bacterium that causes the zoonotic infection tularemia. While much literature exists on the host response to F. tularensis infection, the vast majority of work has been conducted using attenuated strains of Francisella that do not cause disease in humans.

Post-exposure immunization against Francisella tularensis membrane proteins augments protective efficacy of gentamicin in a mouse model of pneumonic tularemia.

Successful treatment of pneumonic infection with Francisella tularensis, the causative agent of tularemia, requires rapid initiation of antibiotic therapy, yet even then treatment failures may occur. Consequently, new treatments are needed to enhance the effectiveness of antimicrobial therapy for acute pneumonic tularemia. In a prior study, immunization with F.

Rapid detection of the poly-gamma-D-glutamic acid capsular antigen of Bacillus anthracis by latex agglutination.

Latex agglutination has been used to detect capsular polysaccharides from a variety of bacteria in body fluids. A latex agglutination assay was constructed for detection of the poly-gamma-D-glutamic acid (gammaDPGA) capsular polypeptide of Bacillus anthracis in serum from animal models of pulmonary anthrax. The assay was able to detect gammaDPGA in serum from infected animals at concentrations of 100 to 200 ng/mL.

Macrophage uptake, intracellular localization, and degradation of poly-gamma-D-glutamic acid, the capsular antigen of Bacillus anthracis.

Bacillus anthracis is surrounded by a capsular polypeptide composed of poly-gamma-D-glutamic acid (PGA). This antiphagocytic capsule is an essential virulence factor and is shed into body fluids during a murine model of pulmonary anthrax. Our previous studies of a murine model for antigen clearance showed that purified PGA accumulates in the liver and spleen, most notably in splenic macrophages and the Kupffer cells and sinusoidal endothelial cells of the liver.

In vivo fate and distribution of poly-gamma-D-glutamic acid, the capsular antigen from Bacillus anthracis.

Bacillus anthracis is surrounded by an antiphagocytic capsule composed of poly-gamma-d-glutamic acid (gammaDPGA). Bacterial and fungal capsular polysaccharides are shed into body fluids in large amounts during infection. The goal of our study was to examine the in vivo fate and distribution of the gammaDPGA capsular polypeptide.