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Chapter 18 : Resistance of Bacterial Spores

Author: Peter Setlow1
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Affiliations: 1: Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030–3305
Content Type: Monograph
Publication Year: 2011

Category: Microbial Genetics and Molecular Biology

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Abstract:

This chapter discusses the resistance of spores of and , with focus species, in which spore resistance mechanisms are best understood, with most specific knowledge from work with spores. The spore coat plays a major role in spore resistance. First, some protective enzymes that are loosely associated with or integral components of the coat can inactivate toxic chemicals; two such enzymes are superoxide dismutase and catalase. Second, coat protein appears to act like ‘’reactive armor’’ detoxifying damaging chemicals before they can react with components in the spore’s interior. Spore structure is important in spore resistance and because spore structure is different than that of growing cells, the major features of spore structure and how these features contribute to spore resistance is outlined in the chapter. Spores of and are more resistant than growing cells to stress factors and studies have attempted to correlate differences in spore resistance with differences in spore structural or biochemical properties. It is reasonable to ask whether conclusions from work on one or two species are applicable to spores of other species, available evidence indicates that basic mechanisms of spore resistance are similar in spores of all and . Some resistance of core proteins to damage, in particular to chemicals, is likely because of mechanisms that also protect DNA, including detoxification of reactive chemicals by enzymes in the coat/exosporium, inactivation of toxic chemicals by reaction with coat components, and the low permeability of the inner membrane.

Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
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Resistance of Bacterial Spores
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Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
/content/10.1128/9781555816841.ch18.ch18fig01
Figure 1.
Schematic structure of a / spore. Spore layers are not drawn to scale, the exosporium is not present on spores of some species, and spores of some species have large appendages arising from the exosporium or coat.
10.1128/9781555816841/f0320-01_thmb.gif
10.1128/9781555816841/f0320-01.gif
Image of Figure 1.
Figure 1.

Schematic structure of a / spore. Spore layers are not drawn to scale, the exosporium is not present on spores of some species, and spores of some species have large appendages arising from the exosporium or coat.

Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
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Figure 2.
Amino acid sequences of α/β-type SASPs from various and . Sequences are from one of these proteins in each species and data are from the NCBI database or Gold Tables Online of ongoing bacterial genome sequencing projects. Amino acid residues are shown in the one letter code and the regions highlighted in gray are the two large helical regions in the proteins, the initial region being helix 1 and the second region helix 2. The emboldened Met residue is protected from modification upon α/β-type SASP binding to DNA, the emboldened amino acid doublet with Glu as the first residue is the site cleaved by the SASP-specific protease following spore germination, and the Asn residue in the emboldened NG doublet deamidates rapidly and DNA binding blocks deamidation. The abbreviations for the species are as follows. : Afl, ; Ali, , Bam, ; Ban, ; Bbe, ; Bce, ; Bcl, ; Bco, ; Bfi, ; Bha, ; Bli, ; Bme, ; Bpu, ; Bsu, ; Bth, ; Bwe, ; Gka, ; Gst, ; Gth, ; Lsp, ; Oih, ; Pjd, ; and Pla, species are: Cac, ; Cba, ; Cbe, ; Cbo, ; Cbu, ; Cce, ; Cdi, ; Ckl, ; Cle, ; Cno, ; Cpe, ; Cph, ; Cra, ; Csp, ; Cso, , Cte, ; and Cth, . Note also that many α/β-type SASPs sequences available from are not shown here.
10.1128/9781555816841/f0322-01_thmb.gif
10.1128/9781555816841/f0322-01.gif
Image of Figure 2.
Figure 2.

Amino acid sequences of α/β-type SASPs from various and . Sequences are from one of these proteins in each species and data are from the NCBI database or Gold Tables Online of ongoing bacterial genome sequencing projects. Amino acid residues are shown in the one letter code and the regions highlighted in gray are the two large helical regions in the proteins, the initial region being helix 1 and the second region helix 2. The emboldened Met residue is protected from modification upon α/β-type SASP binding to DNA, the emboldened amino acid doublet with Glu as the first residue is the site cleaved by the SASP-specific protease following spore germination, and the Asn residue in the emboldened NG doublet deamidates rapidly and DNA binding blocks deamidation. The abbreviations for the species are as follows. : Afl, ; Ali, , Bam, ; Ban, ; Bbe, ; Bce, ; Bcl, ; Bco, ; Bfi, ; Bha, ; Bli, ; Bme, ; Bpu, ; Bsu, ; Bth, ; Bwe, ; Gka, ; Gst, ; Gth, ; Lsp, ; Oih, ; Pjd, ; and Pla, species are: Cac, ; Cba, ; Cbe, ; Cbo, ; Cbu, ; Cce, ; Cdi, ; Ckl, ; Cle, ; Cno, ; Cpe, ; Cph, ; Cra, ; Csp, ; Cso, , Cte, ; and Cth, . Note also that many α/β-type SASPs sequences available from are not shown here.

Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
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Figure 3.
Structure of dipicolinic acid (DPA). At physiological pH, both carboxyl groups will be ionized, allowing DPA to chelate divalent metal ions, in particular Ca.
10.1128/9781555816841/f0323-01_thmb.gif
10.1128/9781555816841/f0323-01.gif
Image of Figure 3.
Figure 3.

Structure of dipicolinic acid (DPA). At physiological pH, both carboxyl groups will be ionized, allowing DPA to chelate divalent metal ions, in particular Ca.

Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
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Tables

Resistance of Bacterial Spores
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Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
/content/10.1128/9781555816841.ch18.ch18table01
Table 1.
Essential spore components that are targets for lethal damage
Generic image for table
Table 1.

Essential spore components that are targets for lethal damage

Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
/content/10.1128/9781555816841.ch18.ch18table02
Table 2.
Factors important in protecting essential spore components
Generic image for table
Table 2.

Factors important in protecting essential spore components

Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
/content/10.1128/9781555816841.ch18.ch18table03
Table 3.
Resistance properties of spores and growing cells of strains
Generic image for table
Table 3.

Resistance properties of spores and growing cells of strains

Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18
/content/10.1128/9781555816841.ch18.ch18table04
Table 4.
DNA photoproducts from UV irradiated spores of various strains
Generic image for table
Table 4.

DNA photoproducts from UV irradiated spores of various strains

Citation: Setlow P. 2011. Resistance of Bacterial Spores, p 319-332. In Storz G, Hengge R (ed), Bacterial Stress Responses, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555816841.ch18

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