pleuropneumonia/protease

Actinobacillus pleuropneumoniae serotype 1 releases vesicles containing proteases and Apx toxins into the culture medium. Vesicles were concentrated by ultracentrifugation and analyzed by electron microscopy and electrophoresis; their size ranged from 20 to 200 nm. A polyclonal antiserum raised

Mannheimia haemolytica colonizes the nasopharynx of cattle and can cause severe fibrinous pleuropneumonia. IgA proteases are metalloendopeptidases released by bacteria that cleave IgA, enhancing colonization of mucosa. The objectives of these studies were to characterize M. haemolytica IgA1 and IgA2

Actinobacillus pleuropneumoniae is the etiological agent of porcine pleuropneumonia, a highly contagious respiratory infection in pigs. AasP, a putative subtilisin-like serine protease autotransporter, has recently been identified in A. pleuropneumoniae. We hypothesized that, similarly to other

Actinobacillus pleuropneumoniae (App) is a Gram-negative bacterium that causes porcine pleuropneumonia, leading to economic losses in the swine industry. Due to bacterial resistance to antibiotics, new treatments for this disease are currently being sought. Lactoferrin (Lf) is an innate immune

There have been three basic approaches to vaccine development: inactivated, live attenuated, and purified cell component vaccines. With rare exception, inactivated vaccines have proved disappointing. Because men and animals recovering from naturally occurring diseases are resistant to rechallenge,

Actinobacillus pleuropneumoniae is the causal agent of porcine contagious pleuropneumonia (PCP). The infection produces important economic losses in porciculture due to its high morbidity and mortality. Survivors are asymptomatic carriers infectious to other pigs and have low alimentary conversion.

Actinobacillus pleuropneumoniae causes pleuropneumonia in swine. This bacterium secretes proteases that degrade porcine hemoglobin and IgA in vitro. To further characterize A. pleuropneumoniae proteases, we constructed a genomic library expressed in Escherichia coli DH5alpha, and selected a clone

The complete amino acid and nucleotide sequence of a secreted metalloprotease produced by Actinobacillus pleuropneumoniae serotype 1 is reported. A clone showing proteolytic activity in cell-free culture media was selected from a genomic library of A. pleuropneumoniae serotype 1 in pUC 19. The