Serum-Mediated Cleavage of Bacillus anthracis Protective Antigen Is a Two-Step Process That Involves a Serum Carboxypeptidase
Year: 2018
Type: article
Abstract: Much our understanding of the activity of anthrax toxin is based on in-vitro systems, which delineate the interaction between B. anthracis toxins and the cell surface. These systems however, fail to account for the intimate association of B. anthracis with the circulatory system, including the contribution of serum proteins to the host response and processing of anthrax toxins. Using variety immunologic techniques to inhibit serum processing of B. anthracis Protective Antigen (PA) along with mass spectrometry analysis, we demonstrate that serum digests PA via 2 distinct reactions. In the first reaction, serum cleaves PA 83 into 2 fragments to produce PA 63 and PA 20 fragments, similar to that observed following furin digestion. This is followed by carboxypeptidase-mediated removal of the carboxy-terminal arginine and lysine residues from PA 20 .
Source: mSphere
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,500
Awards: G1558937058, G177305599, Immunodiagnostic Tests for the Rapid Diagnosis of Tb, G2436179761, Synergy of Host Defense Mechanisms in the Lung, G2773611754, G3325981176, G356915196, G4559384, G4617214234, G6126703269, Antibodies associated with protection against tuberculosis in nonhuman primates, G624453842, Protective antibodies for Cryptococcal Infections, Mass Spectrometer System, Biology of Fungal Melanin, Northeast Biodefense Center, G9000068980, G9000075020, G9000079094, G9000096188, G9000237099, G9000324242, Molecular Characterization of C. neoformans Antibodies
OpenAlex ID: W2949345223