Characterization of the spore surface and exosporium proteins of Clostridium sporogenes; implications for Clostridium botulinum group I strains.
Characterization of the spore surface and exosporium proteins of Clostridium sporogenes; implications for Clostridium botulinum group I strains.
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DOI:
10.1016/j.fm.2016.06.003
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发表时间:
2016-10
影响因子:
5.3
通讯作者:
Bullough PA
中科院分区:
文献类型:
--
作者:
Janganan TK;Mullin N;Tzokov SB;Stringer S;Fagan RP;Hobbs JK;Moir A;Bullough PA
Clostridium sporogenes is a non-pathogenic close relative and surrogate for Group I (proteolytic) neurotoxin-producing Clostridium botulinum strains. The exosporium, the sac-like outermost layer of spores of these species, is likely to contribute to adhesion, dissemination, and virulence. A paracrystalline array, hairy nap, and several appendages were detected in the exosporium of C. sporogenes strain NCIMB 701792 by EM and AFM. The protein composition of purified exosporium was explored by LC-MS/MS of tryptic peptides from major individual SDS-PAGE-separated protein bands, and from bulk exosporium. Two high molecular weight protein bands both contained the same protein with a collagen-like repeat domain, the probable constituent of the hairy nap, as well as cysteine-rich proteins CsxA and CsxB. A third cysteine-rich protein (CsxC) was also identified. These three proteins are also encoded in C. botulinum Prevot 594, and homologues (75–100% amino acid identity) are encoded in many other Group I strains. This work provides the first insight into the likely composition and organization of the exosporium of Group I C. botulinum spores. Clostridium sporogenes spores have a paracrystalline outer surface (exosporium). The spore surface is decorated with a variety of filaments and appendages. Appendages include long beaded filaments of unknown function. BclA-like exosporium proteins with collagen-like repeat domains are present. Novel cysteine-rich exosporium proteins may compose the exosporium basal array.