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function relationships is critical to determining mechanisms of pathogenesis,
environmental resistance, immune response and spore's physicochemical
properties. Thus, the development and application of high-resolution imaging
techniques, which could address spatially explicit bacterial spore coat protein
architecture at nanometre resolution under physiological conditions, are of
considerable importance.
We have directly visualized species-speciic high-resolution native spore
coat structures of bacterial spores including the exosporium and crystalline
layers of the spore coat ( Fig. 4.3 ) of various
Bacillus 4-7,10-12
and
C. novyi-NT 8
species in their natural environment, namely, air and luid.
(a)
(b)
(c)
(d)
(e)
(f)
Figure 4.3. High-resolution spore coat structures of Bacillus spores. The outer spore
coats of B. atrophaeus (a,b), B. cereus (c) and B. thuringiensis (d) consist of crystalline
layers rodlet and honeycomb structures.
spores contain a crystalline
honeycomb structure (e) beneath the exterior rodlet layer (c). B. thuringiensis spore
coats do not contain rodlet structures. Rodlet assemblies can be seen adsorbed to the
substrate (f ). Images reproduced, with permission from Ref. 4. © (2005) Biophysical
Society, USA.
B. cereus
( Fig. 4.3a,b ) , the outer spore coat was composed
of a crystalline rodlet layer with a periodicity of ~8 nm. In case of
For
Bacillus atrophaeus
Bacillus
subtilis
spores, the rodlet structure was typically completely or partially
covered by the amorphous layer ( Fig. 4.4a ) . Patches of amorphous layer were
also occasionally seen on
B. atrophaeus
spores.
Removal of the
Bacillus cereus
and
B. thuringiensis
exosporium by sonication 4 or single-cell French Press
 
 
 
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