Diverse supramolecular structures formed by self‐assembling proteins of the <scp><i>B</i></scp><i>acillus subtilis</i> spore coat

Jiang, Shuo; Wan, Qiang; Krajcikova, Daniela; Tang, Jilin; Tzokov, Svetomir B.; Barák, Imrich; Bullough, Per A.

doi:10.1111/mmi.13030

Cited by 44 publications

(76 citation statements)

References 69 publications

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“…3a 2 , white arrows) were measured in a range from 40 to 90 nm (n = 20). These results are in good agreement with electron micrographs of typical CotE aggregates, displaying extended net-like structures (Jiang et al, 2015). However, the average repeat spacing was about 15 nm, although the mesh size was highly variable.…”

Section: Assembly Of Cote and Cotz On Silicon Substrate In Vitrosupporting

confidence: 84%

Physical interaction and assembly of Bacillus subtilis spore coat proteins CotE and CotZ studied by atomic force microscopy

Liu

Qiao

Krajcikova

et al. 2016

Journal of Structural Biology

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The spore of Bacillus subtilis, a dormant type of cell, is surrounded by a complex multilayered protein structure known as the coat. It is composed of over 70 proteins and essential for the spore to withstand extreme environmental conditions and allow germination under favorable conditions. However, understanding how the properties of the coat arise from the interactions among all these proteins is an important challenge. Moreover, many specific protein-protein interactions among the coat proteins are crucial for coat assembly. In this study, atomic force microscopy (AFM) based single molecule force spectroscopy (SMFS) was applied to investigate the interaction as a dynamic process between two morphogenetic coat proteins, CotE and CotZ. The unbinding force and kinetic parameters characterizing the interaction between CotE and CotZ were obtained. It is found that there is a strong affinity between CotE and CotZ. Furthermore, the assembly behaviors of CotE and CotZ, individually or in combination, were studied by AFM at solid-liquid interfaces. Our results revealed that CotE-CotZ assembly is dependent on their molar ratios and the interaction between CotE and CotZ involves in the CotE-CotZ assembly.

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Section: Assembly Of Cote and Cotz On Silicon Substrate In Vitrosupporting

confidence: 84%

Physical interaction and assembly of Bacillus subtilis spore coat proteins CotE and CotZ studied by atomic force microscopy

Liu

Qiao

Krajcikova

et al. 2016

Journal of Structural Biology

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“…Figure B shows that both heat and reducing agent are required for the complete loss of detectable hexamer. We previously found analogous behaviour for CotY Bs hexamers and showed that higher order assemblies also required reducing agent for disassembly (Jiang et al ., ). Treatment of rExsY crystals with a combination of both heat and DTT was required to destroy any ordered crystallinity.…”

Section: Discussionmentioning

confidence: 97%

“…Our studies of coat proteins in B. subtilis suggest that self‐organization plays a very significant role in spore construction (Jiang et al ., ). Does self‐assembly play a role in the extension of the exosporium around the nascent spore?…”

Section: Introductionmentioning

confidence: 97%

Molecular tiling on the surface of a bacterial spore – the exosporium of the Bacillus anthracis/cereus/thuringiensis group

Terry

Jiang

Radford

et al. 2017

Molecular Microbiology

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SummaryBacteria of the genera Bacillus and Clostridium form highly resistant spores, which in the case of some pathogens act as the infectious agents. An exosporium forms the outermost layer of some spores; it plays roles in protection, adhesion, dissemination, host targeting in pathogens and germination control. The exosporium of the Bacillus cereus group, including the anthrax pathogen, contains a 2D‐crystalline basal layer, overlaid by a hairy nap. BclA and related proteins form the hairy nap, and require ExsFA (BxpB) for their localization on the basal layer. Until now, the identity of the main structural protein components of the basal layer was unknown. We demonstrate here that ExsY forms one of the essential components. Through heterologous expression in Escherichia coli, we also demonstrate that ExsY can self‐assemble into ordered 2D arrays that mimic the structure of the exosporium basal layer. Self‐assembly is likely to play an important role in the construction of the exosporium. The ExsY array is stable to heat and chemical denaturants, forming a robust layer that would contribute to overall spore resistance. Our structural analysis also provides novel insight into the location of other molecular components anchored onto the exosporium, such as BclA and ExsFA.

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“…These proteins form one-dimensional fibers, two-dimensional sheets, and three-dimensional stacks. With CotY, the mode of assembly resembles that of the exosporium basal layer described for B. anthracis and B. cereus (55). CotY is a component of the B. subtilis crust layer and the B. cereus group exosporium layer.…”

Section: The Spore Crust Layermentioning

confidence: 99%

“…Interestingly, the CotZ protein, which plays a role in the assembly of the crust layer of B. subtilis, displays sequence similarity to the ExsY protein (35% identity and 46% similarity over 141 residues), a protein involved in exosporium assembly in B. anthracis (42). B. subtilis CotE, CotV, CotY, and CotW coat proteins expressed in Escherichia coli can self-assemble intracellularly into stable complexes (55). These proteins form one-dimensional fibers, two-dimensional sheets, and three-dimensional stacks.…”

Section: The Spore Crust Layermentioning

confidence: 99%

The Exosporium Layer of Bacterial Spores: a Connection to the Environment and the Infected Host

Stewart

2015

Microbiol Mol Biol Rev

138

155

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SUMMARYMuch of what we know regarding bacterial spore structure and function has been learned from studies of the genetically well-characterized bacteriumBacillus subtilis. Molecular aspects of spore structure, assembly, and function are well defined. However, certain bacteria produce spores with an outer spore layer, the exosporium, which is not present onB. subtilisspores. Our understanding of the composition and biological functions of the exosporium layer is much more limited than that of other aspects of the spore. Because the bacterial spore surface is important for the spore's interactions with the environment, as well as being the site of interaction of the spore with the host's innate immune system in the case of spore-forming bacterial pathogens, the exosporium is worthy of continued investigation. Recent exosporium studies have focused largely on members of theBacillus cereusfamily, principallyBacillus anthracisandBacillus cereus. Our understanding of the composition of the exosporium, the pathway of its assembly, and its role in spore biology is now coming into sharper focus. This review expands on a 2007 review of spore surface layers which provided an excellent conceptual framework of exosporium structure and function (A. O. Henriques and C. P. Moran, Jr., Annu Rev Microbiol61:555–588, 2007,http://dx.doi.org/10.1146/annurev.micro.61.080706.093224). That review began a process of considering outer spore layers as an integrated, multilayered structure rather than simply regarding the outer spore components as independent parts.

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Diverse supramolecular structures formed by self‐assembling proteins of the Bacillus subtilis spore coat

Cited by 44 publications

References 69 publications

Physical interaction and assembly of Bacillus subtilis spore coat proteins CotE and CotZ studied by atomic force microscopy

Physical interaction and assembly of Bacillus subtilis spore coat proteins CotE and CotZ studied by atomic force microscopy

Molecular tiling on the surface of a bacterial spore – the exosporium of the Bacillus anthracis/cereus/thuringiensis group

The Exosporium Layer of Bacterial Spores: a Connection to the Environment and the Infected Host

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