Disease relevance of AIDS003574

• Bacillus anthracis, the agent of anthrax, produces a poly-D-glutamic acid capsule that has been implicated in virulence [1].
• Bacillus anthracis produces a gamma-linked poly-D-glutamic acid capsule that is essential for virulence [2].
• Poly-D-glutamic acid induces an acute lysosomal thesaurismosis of proximal tubules and a marked proliferation of interstitium in rat kidney [3].
• In a retrospective investigation, we used enzyme-linked immunosorbent assays to measure antibody titers to components of anthrax edema toxin (edema factor [EF] and protective antigen [PA]), lethal toxin (lethal factor [LF] and PA), and poly-D-glutamic acid capsule [4].

High impact information on AIDS003574

• Over the chosen intervals, from 80 to 96% of the lysosomes could be paired within 1 micron of each other in the NH4Cl- and PGA-treated cells in comparison with 50-70% in normal cells [5].
• Treatment of the macrophages with 5-10 mM NH4Cl for 0.5-2 h or with 100 micrograms PGA/ml for 5 d caused a striking inhibition of saltatory lysosomal movements, as well as the expected inhibition of P-L fusion [5].
• The Dep protein appears to be an enzyme that catalyses the hydrolysis of the poly-D-glutamic acid capsule [2].
• We discovered that brief administration of a low-molecular-weight synthetic peptide, poly-d-glutamic acid (PDG), induced prompt and robust expansion of EPO-producing PIC in rat kidney, without evidence of tubular cell necrosis/apoptosis or fibrotic reaction [6].
• Specimens obtained 3 hours after injection of poly-D-glutamic acid and horseradish peroxidase suggested an impairment of endosome and/or lysosome fission, but not fusion [3].

Chemical compound and disease context of AIDS003574

• The major virulence factors of Bacillus anthracis are a poly-D glutamic acid capsule and a three-component protein exotoxin [7].

Biological context of AIDS003574

• Virulent strains of Bacillus anthracis contain two large plasmids. pXO1 encodes the three component protein exotoxin and pXO2 is necessary for synthesis of the poly-D-glutamic acid capsule [8].

Anatomical context of AIDS003574

• Finally, 1 day after the injection of poly-D-glutamic acid, the activities of several lysosomal enzymes (hexosaminidase, cathepsin B, acid sphingomyelinase, and sulfatase B), but not of all of them (eg, acid phosphatase), were increased in the kidney cortex [9].
• The anti-ssDNA antibodies bound to sheep erythrocytes, ssDNA and, marginally, to trinitrophenyl-gelatin; they did not bind to poly-D-glutamic acid, rat erythrocytes or mouse erythrocytes [10].
• After the PDGA exposure, HSP73 and HSP90 accumulated within enlarged lysosomes of proximal tubular epithelial cells [11].

Analytical, diagnostic and therapeutic context of AIDS003574

• Serum was also tested by enzyme-linked immunosorbent assay (ELISA) for the presence of antibodies to poly-D-glutamic acid capsule [12].

References