The co-dependence of BxpB/ExsFA and BclA for proper incorporation into the exosporium of Bacillus anthracis.

ABSTRACT: The outermost layer of the Bacillus anthracis spore consists of an exosporium comprised of two distinct layers, an outer hair-like nap layer and an internal basal layer. The hair-like nap is primarily comprised of the glycosylated collagen-like protein BclA. BclA is found in a trimeric form in close association with many other exosporium proteins in high-molecular weight complexes. We previously had characterized an N-terminal sequence of BclA that is sufficient for incorporation into the exosporium. Here we utilized site-directed mutagenesis to identify BclA residues critical to two steps in this process, positioning of the protein at the site of the developing exosporium basal layer and stable incorporation which includes a proteolytic cleavage of BclA after residue 19. The BxpB (ExsFA)

SUBMITTER: Thompson BM 

PROVIDER: S-EPMC3044595 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature