期刊
INFECTION AND IMMUNITY
卷 74, 期 7, 页码 4149-4156出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/IAI.00150-06
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资金
- NHLBI NIH HHS [R01 HL059842, HL59842-07] Funding Source: Medline
- NIAID NIH HHS [R01 AI022021, R56 AI060507, R01 AI052733, AI33774-11, R37 AI033142, AI060507, R01 AI033774, AI52733-02, R01 AI033142, AI22021, AI33142-11, R37 AI022021, R01 AI060507] Funding Source: Medline
- NIGMS NIH HHS [GM07142-01] Funding Source: Medline
Antibody (Ab) responses to Bacillus anthracis toxins are protective, but relatively few protective monoclonal antibodies (MAbs) have been reported. Protective antigen (PA) is essential for the action of B. anthracis lethal toxin (LeTx) and edema toxin. In this study, we generated two MAbs to PA, MAbs 7.5G and 10F4. These MAbs did not compete for binding to PA, consistent with specificities for different epitopes. The MAbs were tested for their ability to protect a monolayer of cultured macrophages against toxin-mediated cytotoxicity. MAb 7.5G, the most-neutralizing MAb, bound to domain I of PA and reduced LeTx toxicity in BALB/c mice. Remarkably, MAb 7.5G provided protection without blocking the binding of PA or lethal factor or the formation of the PA heptamer complex. However, MAb 7.5G slowed the proteolytic digestion of PA by furin in vitro, suggesting a potential mechanism for Ab-mediated protection. These observations indicate that some Abs to domain I can contribute to host protection.
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