Document Detail

Treatment of experimental anthrax with recombinant capsule depolymerase.
MedLine Citation:
PMID:  18160516     Owner:  NLM     Status:  MEDLINE    
Bacillus anthracis produces an antiphagocytic gamma-linked poly-D-glutamic acid capsule that is required for virulence. Capsule depolymerase (CapD) is a membrane-associated poly-gamma-glutamate-specific depolymerase encoded on the B. anthracis capsule plasmid, pX02, that is reported to contribute to virulence by anchoring the capsule to the peptidoglycan and partially degrading high-molecular-weight capsule from the bacterial surface. We previously demonstrated that treatment with CapD effectively removes the capsule from anthrax bacilli, rendering them susceptible to phagocytic killing in vitro. Here we report that CapD promoted in vivo phagocytic killing of B. anthracis bacilli by mouse peritoneal neutrophils and that parenteral administration of CapD protected mice in two models of anthrax infection. CapD conferred significant protection compared with controls when coinjected with encapsulated bacilli from fully virulent B. anthracis Ames or the nontoxigenic encapsulated strain Delta Ames and when injected 10 min after infection with encapsulated bacilli from B. anthracis Ames. Protection was also observed when CapD was administered 30 h after infection with B. anthracis Delta Ames spores, while significant protection could not be demonstrated following challenge with B. anthracis Ames spores. These data support the proposed role of capsule in B. anthracis virulence and suggest that strategies to target anthrax bacilli for neutrophil killing may lead to novel postexposure therapies.
Angelo Scorpio; Steven A Tobery; Wilson J Ribot; Arthur M Friedlander
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2007-12-26
Journal Detail:
Title:  Antimicrobial agents and chemotherapy     Volume:  52     ISSN:  0066-4804     ISO Abbreviation:  Antimicrob. Agents Chemother.     Publication Date:  2008 Mar 
Date Detail:
Created Date:  2008-02-26     Completed Date:  2008-09-02     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  0315061     Medline TA:  Antimicrob Agents Chemother     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1014-20     Citation Subset:  IM    
United States Army Medical Research Institute of Infectious Diseases, 1425 Porter Street, Frederick, MD 21702, USA.
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MeSH Terms
Anthrax / drug therapy*,  microbiology
Bacillus anthracis / drug effects*,  pathogenicity,  physiology
Bacterial Capsules / metabolism*
Glycoside Hydrolases / genetics,  metabolism,  therapeutic use*
Mice, Inbred BALB C
Neutrophils / immunology
Recombinant Proteins / genetics,  metabolism,  therapeutic use*
Spores, Bacterial / physiology
Treatment Outcome
Reg. No./Substance:
0/Recombinant Proteins; EC 3.2.1.-/Glycoside Hydrolases; EC galactohydrolase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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