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can you explain why Bacillus anthracis can be pathogenic in a mouse and not be fought off by the immune system? I need help finding the answer in the article and explain in short answer  link to article: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC106848/

can you explain why Bacillus anthracis can be pathogenic in a mouse and not be fought off by the immune system? I need help finding the answer in the article and explain in short answer  link to article: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC106848/

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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can you explain why Bacillus anthracis can be pathogenic in a mouse and not be fought off by the immune system?

I need help finding the answer in the article and explain in short answer 

link to article: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC106848/

 

VOL. 180, 1998 94 67 43 30- 20- 1 2 3 4 5 6 7 8 FIG. 6. In vivo expression of the two B. anthracis S-layer components. Im- munoblotting of pellet fractions (odd-numbered lanes) and supernatant fractions (even-numbered lanes) of S-layers from wild-type (CAF10) (lanes 1 and 2), Asap (CBA91) (lanes 3 and 4), Aeag (CSM91) (lanes 5 and 6), and Aeag Asap (CSM11) (lanes 7 and 8) strains was carried out with pooled sera from mice infected with the CAF10 strain. Molecular masses are indicated in kilodaltons on the left. shown). EA1 and Sap were found to be major surface antigens, showing that both EA1 and Sap can be synthesized by a cap- sulated strain in vivo. DISCUSSION Although various bacteria from natural environments pos- sess both a capsule and an S-layer, their cosynthesis or struc- tural relationship has rarely been studied (15). B. anthracis has a rather unusual capsule: it is composed not of polysaccharide but of poly-y-D-glutamic acid (13). This bac- terium also has an S-layer, previously evidenced only in cap- sule-free strains (10, 16). Another gram-positive bacterium, B. licheniformis, apparently shares these features, namely, a poly- y-D-glutamic acid capsule and an S-layer (9, 33). However, this B. licheniformis strain, in which the S-layer component is very similar to EA1 (20), seems to lack a capsule. We therefore investigated whether these two structures, the capsule and the S-layer, were exclusive. We found that B. anthracis bacilli syn- thesize EA1, Sap, and the capsule both in vivo and in vitro. Furthermore, the capsule and a structured S-layer were found to be simultaneously present on the bacterial surface, the cap- sule covering the S-layer. Thus, B. anthracis displays a highly complex ultrastructural cell wall architecture. The coexistence of the capsule and the S-layer could have indicated a structural dependence. Such was not the case, as the S-layer was found in noncapsulated strains and the capsule was present on the EA1-Sap double deletion mutant. These results further suggest that the capsule is anchored either to the peptidoglycan-containing sacculus or to the cytoplasmic membrane, independently of the S-layer. However, the fine structure of the capsule may depend on the presence of the underlying S-layer: the S-layer may modify the arborescence of the poly-y-D-glutamic acid fibers. That these structures can be independently synthesized and formed does not exclude func- tional interactions. Pathogenic organisms have various strategies to escape host recognition. One such strategy, which is widespread, is anti- genic variation of exposed proteins, including S-layer proteins. For example, in Campylobacter fetus, genetic rearrangements enable the bacterium to change S-layer components (2, 5). The variants can therefore multiply before the antibody response has developed against the new protein. No gene rearrange- ment between the B. anthracis S-layer genes has been observed (data not shown). The absence of immunolabeling on B. an- thracis whole cells (Fig. 4B and D) in the presence of the capsule suggests that the cell surface is inaccessible to antibod BACILLUS ANTHRACIS CAPSULE AND S-LAYER 57 ies. The presence of anti-EA1 and anti-Sap antibodies in the sera of mice inoculated with strain CAF10 (Fig. 6) indicates that these proteins are synthesized in vivo by the capsulated strain. The presence of these antibodies could be due to the synthesis of these proteins prior to the complete coverage of the surface by the capsule or to leakage or bacterial lysis. Interestingly, the capsule seems to function as a "one-way" filter. EA1 and Sap are not accessible to antibodies from the outside, whereas the three toxin components (protective anti- gen, lethal factor, and edema factor) and Sap are found in culture supernatants of capsulated strains, suggesting that they diffuse from the cell through the capsule to the extracellular medium. The S-layer may have a protective role in the absence of the capsule. It could also be a molecular sieve or could have a still more structural role, delimiting the periplasm, as recently de- scribed for gram-positive bacteria (1, 11). ACKNOWLEDGMENTS We are grateful to A. L. Sonenshein for critical reading of the manuscript. We thank B. Chavinier-Jove and C. Rolin for excellent technical assistance with electron microscopy experiments and photo- graphic prints, respectively. S.M. was supported by the Ministère de l'Enseignement Supérieur et de la Recherche. REFERENCES 1. Beveridge, T. J. 1995. The periplasmic space and the periplasm in gram- positive and gram-negative bacteria. ASM News 61:125-130. 2. Blaser, M. J., E. Wang, M. K. R. Tummuru, R. Washburn, S. Fujimoto, and A. Labigne. 1994. High frequency S-layer protein variation in Campylobacter fetus revealed by sapA mutagenesis. Mol. Microbiol. 14:521-532. Jonas Jon 3. Carlemalm, E., R. M. Garavito, and W. Villiger. 1982. Resin development for electron microscopy and an analysis of embedding at low temperature. J. Microsc. 126:123. 4. Duguid, J. P. 1951. The demonstration of bacterial capsules and slime. J. Pathol. Bacteriol. 63:673-685. 5. Dworkin, J., and M. J. Blaser. 1997. Nested DNA inversion as a paradigm of programmed gene rearrangement. Proc. Natl. Acad. Sci. USA 94:985-990. 6. Etienne-Toumelin, I., J.-C. Sirard, E. Duflot, M. Mock, and A. Fouet. 1995. Characterization of the Bacillus anthracis S-layer: cloning and sequencing of the structural gene. J. Bacteriol. 177:614-620. 7. Farchaus, J. W., W. J. Ribot, M. B. Downs, and J. W. Ezzell. 1995. Purifi- cation and characterization of the major surface array protein from the avirulent Bacillus anthracis Delta Sterne-1. J. Bacteriol. 177:2481-2489. 8. Fouet, A., and M. Mock. 1996. Differential influence of the two Bacillus anthracis plasmids on regulation of virulence gene expression. Infect. Im- mun. 64:4928-4932. 9. Gardner, J. M., and F. A. Troy. 1979. Chemistry and biosynthesis of the poly (y-D-glutamyl) capsule in Bacillus licheniformis. Activation, racemization, and polymerization of glutamic acid by a membranous polyglutamyl syn- thetase complex. J. Biol. Chem. 254:6262-6269. 10. Gerhardt, P. 1967. Cytology of Bacillus anthracis. Fed. Proc. 26:1504-1517. 11. Graham, L. L., T. J. Beveridge, and N. Nanninga. 1991. Periplasmic space and the concept of periplasm. Trends Biochem. Sci. 16:328-329. 12. Green, B. D., L. Battisti, T. M. Koehler, C. B. Thorne, and B. E. Ivins. 1985. Demonstration of a capsule plasmid in Bacillus anthracis. Infect. Immun. 49:291-297. T 13. Hanby, W. E., and H. N. Rydon. 1946. The capsular substance of Bacillus anthracis. Biochem. J. 40:297-309. tra 14. Hayat, M. A. 1981. Fixation for electron microscopy, p. 110-111. Academic Press, Inc., New York, N.Y. ress, 15. Hoiczyk, E., and W. Baumeister. 1995. Envelope structure of four gliding filamentous cyanobacteria. J. Bacteriol. 177:2387-2395. mant 16. Holt, S. C., and E. R. Leadbetter. 1969. Comparative ultrastructure of se- lected aerobic spore-forming bacteria: a freeze-etching study. Bacteriol. Rev. 33:346-378. 17. Karnovsky, M. J. 1965. A formaldehyde-glutaraldehyde fixative of high os- molarity for use in electron microscopy. J. Cell Biol. 27:137A. 18. Keppie, J., H. Smith, and P. W. Harris-Smith. 1953. The chemical basis of the virulence of Bacillus anthracis. II. Some biological properties of bacterial products. Br. J. Exp. Pathol. 34:486-496. 19. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. 20. Mesnage, S., E. Tosi-Couture, M. Mock, P. Gounon, and A. Fouet. 1997. Molecular characterization of the Bacillus anthracis main S-laver compo
Transcribed Image Text:VOL. 180, 1998 94 67 43 30- 20- 1 2 3 4 5 6 7 8 FIG. 6. In vivo expression of the two B. anthracis S-layer components. Im- munoblotting of pellet fractions (odd-numbered lanes) and supernatant fractions (even-numbered lanes) of S-layers from wild-type (CAF10) (lanes 1 and 2), Asap (CBA91) (lanes 3 and 4), Aeag (CSM91) (lanes 5 and 6), and Aeag Asap (CSM11) (lanes 7 and 8) strains was carried out with pooled sera from mice infected with the CAF10 strain. Molecular masses are indicated in kilodaltons on the left. shown). EA1 and Sap were found to be major surface antigens, showing that both EA1 and Sap can be synthesized by a cap- sulated strain in vivo. DISCUSSION Although various bacteria from natural environments pos- sess both a capsule and an S-layer, their cosynthesis or struc- tural relationship has rarely been studied (15). B. anthracis has a rather unusual capsule: it is composed not of polysaccharide but of poly-y-D-glutamic acid (13). This bac- terium also has an S-layer, previously evidenced only in cap- sule-free strains (10, 16). Another gram-positive bacterium, B. licheniformis, apparently shares these features, namely, a poly- y-D-glutamic acid capsule and an S-layer (9, 33). However, this B. licheniformis strain, in which the S-layer component is very similar to EA1 (20), seems to lack a capsule. We therefore investigated whether these two structures, the capsule and the S-layer, were exclusive. We found that B. anthracis bacilli syn- thesize EA1, Sap, and the capsule both in vivo and in vitro. Furthermore, the capsule and a structured S-layer were found to be simultaneously present on the bacterial surface, the cap- sule covering the S-layer. Thus, B. anthracis displays a highly complex ultrastructural cell wall architecture. The coexistence of the capsule and the S-layer could have indicated a structural dependence. Such was not the case, as the S-layer was found in noncapsulated strains and the capsule was present on the EA1-Sap double deletion mutant. These results further suggest that the capsule is anchored either to the peptidoglycan-containing sacculus or to the cytoplasmic membrane, independently of the S-layer. However, the fine structure of the capsule may depend on the presence of the underlying S-layer: the S-layer may modify the arborescence of the poly-y-D-glutamic acid fibers. That these structures can be independently synthesized and formed does not exclude func- tional interactions. Pathogenic organisms have various strategies to escape host recognition. One such strategy, which is widespread, is anti- genic variation of exposed proteins, including S-layer proteins. For example, in Campylobacter fetus, genetic rearrangements enable the bacterium to change S-layer components (2, 5). The variants can therefore multiply before the antibody response has developed against the new protein. No gene rearrange- ment between the B. anthracis S-layer genes has been observed (data not shown). The absence of immunolabeling on B. an- thracis whole cells (Fig. 4B and D) in the presence of the capsule suggests that the cell surface is inaccessible to antibod BACILLUS ANTHRACIS CAPSULE AND S-LAYER 57 ies. The presence of anti-EA1 and anti-Sap antibodies in the sera of mice inoculated with strain CAF10 (Fig. 6) indicates that these proteins are synthesized in vivo by the capsulated strain. The presence of these antibodies could be due to the synthesis of these proteins prior to the complete coverage of the surface by the capsule or to leakage or bacterial lysis. Interestingly, the capsule seems to function as a "one-way" filter. EA1 and Sap are not accessible to antibodies from the outside, whereas the three toxin components (protective anti- gen, lethal factor, and edema factor) and Sap are found in culture supernatants of capsulated strains, suggesting that they diffuse from the cell through the capsule to the extracellular medium. The S-layer may have a protective role in the absence of the capsule. It could also be a molecular sieve or could have a still more structural role, delimiting the periplasm, as recently de- scribed for gram-positive bacteria (1, 11). ACKNOWLEDGMENTS We are grateful to A. L. Sonenshein for critical reading of the manuscript. We thank B. Chavinier-Jove and C. Rolin for excellent technical assistance with electron microscopy experiments and photo- graphic prints, respectively. S.M. was supported by the Ministère de l'Enseignement Supérieur et de la Recherche. REFERENCES 1. Beveridge, T. J. 1995. The periplasmic space and the periplasm in gram- positive and gram-negative bacteria. ASM News 61:125-130. 2. Blaser, M. J., E. Wang, M. K. R. Tummuru, R. Washburn, S. Fujimoto, and A. Labigne. 1994. High frequency S-layer protein variation in Campylobacter fetus revealed by sapA mutagenesis. Mol. Microbiol. 14:521-532. Jonas Jon 3. Carlemalm, E., R. M. Garavito, and W. Villiger. 1982. Resin development for electron microscopy and an analysis of embedding at low temperature. J. Microsc. 126:123. 4. Duguid, J. P. 1951. The demonstration of bacterial capsules and slime. J. Pathol. Bacteriol. 63:673-685. 5. Dworkin, J., and M. J. Blaser. 1997. Nested DNA inversion as a paradigm of programmed gene rearrangement. Proc. Natl. Acad. Sci. USA 94:985-990. 6. Etienne-Toumelin, I., J.-C. Sirard, E. Duflot, M. Mock, and A. Fouet. 1995. Characterization of the Bacillus anthracis S-layer: cloning and sequencing of the structural gene. J. Bacteriol. 177:614-620. 7. Farchaus, J. W., W. J. Ribot, M. B. Downs, and J. W. Ezzell. 1995. Purifi- cation and characterization of the major surface array protein from the avirulent Bacillus anthracis Delta Sterne-1. J. Bacteriol. 177:2481-2489. 8. Fouet, A., and M. Mock. 1996. Differential influence of the two Bacillus anthracis plasmids on regulation of virulence gene expression. Infect. Im- mun. 64:4928-4932. 9. Gardner, J. M., and F. A. Troy. 1979. Chemistry and biosynthesis of the poly (y-D-glutamyl) capsule in Bacillus licheniformis. Activation, racemization, and polymerization of glutamic acid by a membranous polyglutamyl syn- thetase complex. J. Biol. Chem. 254:6262-6269. 10. Gerhardt, P. 1967. Cytology of Bacillus anthracis. Fed. Proc. 26:1504-1517. 11. Graham, L. L., T. J. Beveridge, and N. Nanninga. 1991. Periplasmic space and the concept of periplasm. Trends Biochem. Sci. 16:328-329. 12. Green, B. D., L. Battisti, T. M. Koehler, C. B. Thorne, and B. E. Ivins. 1985. Demonstration of a capsule plasmid in Bacillus anthracis. Infect. Immun. 49:291-297. T 13. Hanby, W. E., and H. N. Rydon. 1946. The capsular substance of Bacillus anthracis. Biochem. J. 40:297-309. tra 14. Hayat, M. A. 1981. Fixation for electron microscopy, p. 110-111. Academic Press, Inc., New York, N.Y. ress, 15. Hoiczyk, E., and W. Baumeister. 1995. Envelope structure of four gliding filamentous cyanobacteria. J. Bacteriol. 177:2387-2395. mant 16. Holt, S. C., and E. R. Leadbetter. 1969. Comparative ultrastructure of se- lected aerobic spore-forming bacteria: a freeze-etching study. Bacteriol. Rev. 33:346-378. 17. Karnovsky, M. J. 1965. A formaldehyde-glutaraldehyde fixative of high os- molarity for use in electron microscopy. J. Cell Biol. 27:137A. 18. Keppie, J., H. Smith, and P. W. Harris-Smith. 1953. The chemical basis of the virulence of Bacillus anthracis. II. Some biological properties of bacterial products. Br. J. Exp. Pathol. 34:486-496. 19. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. 20. Mesnage, S., E. Tosi-Couture, M. Mock, P. Gounon, and A. Fouet. 1997. Molecular characterization of the Bacillus anthracis main S-laver compo
FIG. 4. Whole-mount noncapsulated (A and C) and capsulated (B and D) CAF10 bacteria immunolabeled with anti-Sap (A and B) and anti-EA1 (C and D) antibodies. Preparations of cultures were incubated with anti-Sap or anti-EA1 antibodies, and binding was revealed with 10-nm gold-conjugated anti-rabbit antibodies. Bar, 1 µm. in conditions inducing capsule synthesis (Fig. 4B and D). La- beling, such as in Fig. 4B, was infrequently observed in prep- arations of capsulated cells and presumably corresponded to the leakage of S-layer components from the bacteria through the capsule. This result indicated that the capsule is distal to the S-layer components and that it completely masks access of the specific antibodies to EA1 and Sap. Capsule and S-layer components can therefore coexist, and the S-layer proteins are localized between the peptidoglycan and the capsule. Analysis of the state of capsulation of strains with a deletion of S-layer component genes. We determined whether the S- layer proteins were required for normal capsulation of the bacteria. Mutants with deletions of the EA1 gene (CSM91), the Sap gene (CBA91), or both eag and sap (CSM11) were constructed as previously described (20) (Table 1). The pellet and supernatant fractions of CAF10 derivatives grown in cap- sule synthesis-inducing conditions were analyzed by polyacryl- amide gel electrophoresis and immunoblotting with anti-EA1 and anti-Sap antibodies (data not shown). The results indi- cated that EA1 and Sap are expressed similarly in the presence and the absence of the capsule and also that, in both cases, Sap is shed into the supernatant. Each strain was grown on CAP plates. The colonies were smooth, suggesting that a capsule was synthesized. The pres- ence of the capsule around the bacteria was confirmed by optical microscopy (Fig. 1A and B). Bacilli from wild-type and S-layer mutants were all capsulated, and no obvious difference in the aspect of capsulation could be seen. The capsule was studied in more detail by electron microscopy (Fig. 3A to D). The micrographs showed that similar amounts of capsule were found around all bacteria tested. This result indicated that the S-layer components, EA1 and Sap, are not required for normal capsulation of B. anthracis bacilli. Coexistence of the capsule and of the structured S-layer. We tested whether EA1 and Sap are organized in a two-dimen- sional crystalline array when covered by the capsule. Thin sections (Fig. 3A to C) suggested that the S-layer proteins were organized in sheaths. The surfaces of strains CAF10 (EA1+ Sap), CBA91 (EA1+), CSM91 (Sap), and CSM11 grown in capsule synthesis-inducing conditions were further analyzed for the presence of structured layers by negative staining (Fig. 5). The cells were vortexed in the presence of glass beads (20). This treatment disrupted the bacteria and tore off the capsule, thus unmasking the S-layers. As expected, no crystalline array was present on the surface of CSM11 cells (data not shown). Conversely, structured layers were clearly visible on CAF10, CBA91, and CSM91 cells (Fig. 5A, B, and C, respectively). This result suggested that in the presence of the capsule, the S-layer components, EA1 and Sap, were able to form struc- tured surface arrays. However, the lattices on these various strains appeared different. The EA1 array was more stable than the Sap array, which was only observed at glutaraldehyde concentrations higher than those required for EA1. In addi- tion, this is the first time that a Sap array has been visualized. Our observations are consistent with the previous suggestion that Sap forms its own, more fragile, structure (20). They also show that the S-layer and capsule structures coexist on the same cell surface. In vivo production of the capsule and the S-layer. To deter- mine whether both the capsule and the S-layer could be pro- duced in vivo, the presence of anti-EA1 and anti-Sap antibod- ies was tested in sera from mice infected with strain CAF10, which is capsulated in vivo (Fig. 6). Sera from infected mice recognized EA1 and Sap but no other bacterial protein under the conditions used. The specificities of the antibodies were confirmed with sera adsorbed onto either EA1 or Sap (data not
Transcribed Image Text:FIG. 4. Whole-mount noncapsulated (A and C) and capsulated (B and D) CAF10 bacteria immunolabeled with anti-Sap (A and B) and anti-EA1 (C and D) antibodies. Preparations of cultures were incubated with anti-Sap or anti-EA1 antibodies, and binding was revealed with 10-nm gold-conjugated anti-rabbit antibodies. Bar, 1 µm. in conditions inducing capsule synthesis (Fig. 4B and D). La- beling, such as in Fig. 4B, was infrequently observed in prep- arations of capsulated cells and presumably corresponded to the leakage of S-layer components from the bacteria through the capsule. This result indicated that the capsule is distal to the S-layer components and that it completely masks access of the specific antibodies to EA1 and Sap. Capsule and S-layer components can therefore coexist, and the S-layer proteins are localized between the peptidoglycan and the capsule. Analysis of the state of capsulation of strains with a deletion of S-layer component genes. We determined whether the S- layer proteins were required for normal capsulation of the bacteria. Mutants with deletions of the EA1 gene (CSM91), the Sap gene (CBA91), or both eag and sap (CSM11) were constructed as previously described (20) (Table 1). The pellet and supernatant fractions of CAF10 derivatives grown in cap- sule synthesis-inducing conditions were analyzed by polyacryl- amide gel electrophoresis and immunoblotting with anti-EA1 and anti-Sap antibodies (data not shown). The results indi- cated that EA1 and Sap are expressed similarly in the presence and the absence of the capsule and also that, in both cases, Sap is shed into the supernatant. Each strain was grown on CAP plates. The colonies were smooth, suggesting that a capsule was synthesized. The pres- ence of the capsule around the bacteria was confirmed by optical microscopy (Fig. 1A and B). Bacilli from wild-type and S-layer mutants were all capsulated, and no obvious difference in the aspect of capsulation could be seen. The capsule was studied in more detail by electron microscopy (Fig. 3A to D). The micrographs showed that similar amounts of capsule were found around all bacteria tested. This result indicated that the S-layer components, EA1 and Sap, are not required for normal capsulation of B. anthracis bacilli. Coexistence of the capsule and of the structured S-layer. We tested whether EA1 and Sap are organized in a two-dimen- sional crystalline array when covered by the capsule. Thin sections (Fig. 3A to C) suggested that the S-layer proteins were organized in sheaths. The surfaces of strains CAF10 (EA1+ Sap), CBA91 (EA1+), CSM91 (Sap), and CSM11 grown in capsule synthesis-inducing conditions were further analyzed for the presence of structured layers by negative staining (Fig. 5). The cells were vortexed in the presence of glass beads (20). This treatment disrupted the bacteria and tore off the capsule, thus unmasking the S-layers. As expected, no crystalline array was present on the surface of CSM11 cells (data not shown). Conversely, structured layers were clearly visible on CAF10, CBA91, and CSM91 cells (Fig. 5A, B, and C, respectively). This result suggested that in the presence of the capsule, the S-layer components, EA1 and Sap, were able to form struc- tured surface arrays. However, the lattices on these various strains appeared different. The EA1 array was more stable than the Sap array, which was only observed at glutaraldehyde concentrations higher than those required for EA1. In addi- tion, this is the first time that a Sap array has been visualized. Our observations are consistent with the previous suggestion that Sap forms its own, more fragile, structure (20). They also show that the S-layer and capsule structures coexist on the same cell surface. In vivo production of the capsule and the S-layer. To deter- mine whether both the capsule and the S-layer could be pro- duced in vivo, the presence of anti-EA1 and anti-Sap antibod- ies was tested in sera from mice infected with strain CAF10, which is capsulated in vivo (Fig. 6). Sera from infected mice recognized EA1 and Sap but no other bacterial protein under the conditions used. The specificities of the antibodies were confirmed with sera adsorbed onto either EA1 or Sap (data not
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