The Structure and Function of Novel Proteins of Bacillus anthracis and Other Spore-Forming Bacteria: Development of Novel Prophylactic and Therapeutic Agents
Author: Mark J. Jedrzejas
Source: Critical Reviews in Biochemistry and Molecular Biology, Volume 37, Number 5, September-October 2002 , pp. 339-373(35)
Publisher: Informa Healthcare
Abstract:
The overall goal of this review is to summarize the current body of knowledge about the structure and function of major proteins of Bacillus anthracis and/or similar spore-forming organisms. B. anthracis is a key spore-forming biological threat agent, as well as human and animal Gram-positive bacterial pathogen. The structural information described here is limited to approximately the last 5 years. This information is then related to the role of the selected proteins in pathogenesis and in the possible development of novel vaccine and/or other antimicrobial agents against spore-forming organisms, including anthrax, a disease caused by B. anthracis. Among spore-forming bacteria, Bacillus and Clostridium species are the predominant spore-forming bacilli that cause serious diseases. The biochemical properties and mechanism of catalysis of the novel spore germination protease that degrades small, acid-soluble proteins protecting DNA against damage, a cofactor independent phosphoglycerate mutase, NAD+ synthetase, and the three know B. anthracis toxins, protective antigen, lethal factor, and edema factor are described. The studies described in this work review and unify selected information critical for the prevention of microbial diseases such as anthrax. A strategy for the structure-guided development of new prophylactic and therapeutic agents is discussed. <kwdg><kwd>anthrax<kwd>bioterrorism<kwd>Clostridium<kwd>drug<kwd>threat agent<kwd>vaccine.Keywords: anthrax; bioterrorism; drug; threat agent; vaccine.
Document Type: Research article
DOI: http://dx.doi.org/10.1080/10409230290771537
Affiliations: 1: Children's Hospital Oakland Research Institute, Oakland, CA 94609
Publication date: 2002-09-01
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