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Chapter 5 : Role of Phosphorylcholine in Respiratory Tract Colonization

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Role of Phosphorylcholine in Respiratory Tract Colonization, Page 1 of 2

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Abstract:

The majority of the homologous sequences were “housekeeping genes” that are widely distributed among both respiratory and nonrespiratory tract bacterial species. It appears that the expression of choline phosphate (ChoP) phosphorylcholine among respiratory tract organisms is an example of convergent evolution since ChoP is present on distinct bacterial structures in different species. An additional consideration is that in each of these species, ChoP is exposed on the bacterial cell surface, suggesting that it plays a role in host-bacterium interaction. The chapter focuses on phosphorylcholine expression. Exchanging the licD genes between the two strains with ChoP on different chain extensions was sufficient to switch its position. Therefore, in addition to the mechanism involving phase variation, structural rearrangements within the oligosaccharide have the potential to aid the evasion of an immune response targeting ChoP. The chapter also discusses the role of ChoP in the host-bacterium interaction and the advantages and disadvantages that expression of this host-like structure may confer on bacterial survival. A series of experiments examined whether bacteria are predominantly ChoP phase-on or phase-off during colonization and systemic infection. The efficacy of the human anti-ChoP IgG was assessed by using in vitro assays that correlate with protection against and infection. The surface expression of ChoP appears to be particularly common among species that colonize predominantly the upper respiratory tract. This allows for bacterial mimicry of the host cell surface since choline is a prominent feature of the host cell membrane.

Citation: Weiser J. 2005. Role of Phosphorylcholine in Respiratory Tract Colonization, p 61-72. In Nataro J, Cohen P, Mobley H, Weiser J (ed), Colonization of Mucosal Surfaces. ASM Press, Washington, DC. doi: 10.1128/9781555817619.ch5

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Figures

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Figure 1

Composite Western immunoblot with MAb TEPC-15, summarizing the common phosphorylcholine epitope on six species of mucosal pathogens and examples of variation in its expression. Lanes: 1 and 2, nontypeable strain H233 phase variants with ChoP and ChoP LPS, respectively; 3, strain R6 lipoteichoic acid; 4 and 5, phase variants of strain Jp-2 without and with ChoP LPS, respectively; 6 to 10, grown at 26.5, 30.0, 33.5, 37.0, and 39.5°C, respectively; 11, purified pilin; 12 to 14, piliated phase variants of strain MS11 without and with the ChoP-LPS. Reprinted from reference 58 with permission from Elsevier.

Citation: Weiser J. 2005. Role of Phosphorylcholine in Respiratory Tract Colonization, p 61-72. In Nataro J, Cohen P, Mobley H, Weiser J (ed), Colonization of Mucosal Surfaces. ASM Press, Washington, DC. doi: 10.1128/9781555817619.ch5
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Figure 2

Current model of the pathway for expression of ChoP in and its proposed interactions within the airway.

Citation: Weiser J. 2005. Role of Phosphorylcholine in Respiratory Tract Colonization, p 61-72. In Nataro J, Cohen P, Mobley H, Weiser J (ed), Colonization of Mucosal Surfaces. ASM Press, Washington, DC. doi: 10.1128/9781555817619.ch5
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Figure 3

When host cells are the sole source of choline, is able to acquire choline by a dependent mechanism. (A) Time course of expression of ChoP on the LPS in bacteria adherent to D562 cells. Strains Rd (ChoP) and Rd:: (ChoP) were allowed to adhere to host epithelial cells in a medium lacking free choline for the period indicted, and the presence of ChoP on the LPS was detected by Western blotting of whole-cell lysates using MAb TEPC-15 to ChoP. (B) GlpQ is required for to transfer choline from host epithelial cells. D562 cells were grown in medium containing [H]choline and infected with the strain indicated (or control without bacteria) for 4 h, and incorporation of the radiolabel was detected in the bacterial fraction as the mean of counts per minute per well ± standard deviation ( 3). Panels A and B reprinted from reference 11 with permission from Blackwell Publishing.

Citation: Weiser J. 2005. Role of Phosphorylcholine in Respiratory Tract Colonization, p 61-72. In Nataro J, Cohen P, Mobley H, Weiser J (ed), Colonization of Mucosal Surfaces. ASM Press, Washington, DC. doi: 10.1128/9781555817619.ch5
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Figure 4

Effect of an rPAF antagonist (PAF-Ra) on bacterial adherence. Adherence of nontypeable or to Detroit 562 pharyngeal epithelial cells in the presence or absence of 1 µM PAF-Ra [1-O-hexadecyl-2-acetyl--glycerol-3-phospho-(-trimethyl)hexanolamine] is expressed as a percentage of the inoculum binding to epithelial cells after 60 min and values represent the means of at least three determinations in duplicate. Error bars indicate standard deviation. Asterisks indicate 0.05 compared to first bar in each panel.

Citation: Weiser J. 2005. Role of Phosphorylcholine in Respiratory Tract Colonization, p 61-72. In Nataro J, Cohen P, Mobley H, Weiser J (ed), Colonization of Mucosal Surfaces. ASM Press, Washington, DC. doi: 10.1128/9781555817619.ch5
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References

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1. Arondel, V.,, C. Benning,, and C. Somerville. 1993. Isolation and functional expression in Escherichia coli of a gene encoding phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. J. Biol. Chem. 268:1600216008.
2. Boman, H. 1991. Antibacterial peptides: key components needed in immunity. Cell 65:205207.
3. Briles, D.,, J. Claflin,, K. Schroer,, and C. Forman. 1981. Mouse IgG3 antibodies are highly protective against infection with Streptococcus pneumoniae. Nature 294:8890.
4. Briles, D. E.,, C. Forman,, J. C. Horowitz,, J. E. Volanakis,, W. J. Benjamin,, L. S. McDaniel,, J. Eldridge,, and J. Brooks. 1989. Antipneumococcal effects of C-reactive protein and monoclonal antibodies to pneumococcal cell wall and capsular antigens. Infect. Immun. 57:14571464.
5. Briles, D. E.,, M. Nahm,, K. Schroer,, J. Davie,, P. Baker,, J. Kearney,, and R. Barletta. 1981. Antiphosphocholine antibodies found in normal mouse serum are protective against intravenous infection with type 3 Streptococcus pneumoniae. J. Exp. Med. 153:694705.
6. Brundish, D. E.,, and J. Baddiley. 1968. Pneumococcal C-substance, a ribitol teichoic acid containing choline phosphate. Biochem. J. 110:573.
7. Cole, A.,, H. Liao,, O. Stuchlik,, J. Tilan,, J. Pohl,, and T. Ganz. 2002. Cationic polypeptides are required for antibacterial activity of human airway fluid. J. Immunol. 169:69856991.
8. Cox, A.,, H. Masoud,, P. Thibault,, J. Brisson,, M. van der Zwan,, M. Perry,, and J. Richards. 2001. Structural analysis of the lipopolysaccharide from the nontypable Haemophilus influenzae strain SB 33. Eur. J. Biochem. 268:52785286.
9. Cundell, D. R.,, N. P. Gerard,, C. Gerard,, I. Idanpaan-Heikkila,, and E. I. Tuomanen. 1995. Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor. Nature 377:435438.
10. Cundell, D. R.,, J. N. Weiser,, J. Shen,, A. Young,, and E. I. Tuomanen. 1995. Relationship between colonial morphology and adherence of Streptococcus pneumoniae. Infect. Immun. 63: 757761.
11. Fan, X.,, H. Goldfine,, E. Lysenko,, and J. Weiser. 2001. The transfer of choline from the host to the bacterial cell surface requires glpQ in Haemophilus influenzae. Mol. Microbiol. 41: 10291036.
12. Fan, X.,, C. Pericone,, E. Lysenko,, H. Goldfine,, and J. Weiser. 2003. Multiple mechanisms for choline transport and utilization in Haemophilus influenzae. Mol. Microbiol. 50:537548.
13. Gillespie, S. H.,, S. Ainscough,, A. Dickens,, and J. Lewin. 1996. Phosphorylcholine-containing antigens in bacteria from the mouth and respiratory tract. J. Med. Microbiol. 44:3540.
14. Gosink, K.,, E. Mann,, C. Guglielmo,, E. Tuomanen,, and H. Masure. 2000. Role of novel choline binding proteins in virulence of Streptococcus pneumoniae. Infect. Immun. 68: 56905695.
15. Gould, J.,, and J. Weiser. 2001. Expression of C-reactive protein in the human respiratory tract. Infect. Immun. 69:17471754.
16. Gould, J.,, and J. Weiser. 2002. The inhibitory effect of C-reactive protein on bacterial phosphorylcholine-platelet activating factor receptor mediated adherence is blocked by surfactant. J. Infect. Dis. 186:361371.
17. Harnett, W.,, and M. Harnett. 1999. Phosphorylcholine: friend or foe of the immune system? Immunol. Today 20:125129.
18. Hulett, M.,, and P. Hogarth. 1994. Molecular basis of Fc receptor function. Adv. Immunol. 57:1127.
19. Janson, H.,, B. Carlen,, A. Cervin,, A. Forsgren,, A. Magnusdottir,, S. Lindberg,, and T. Runer. 1999. Effects on the ciliated epithelium of protein D-producing and -nonproducing nontypeable Haemophilus influenzae in nasopharyngeal tissue cultures. J. Infect. Dis. 180:737746.
20. Janson, H.,, A. Melhus,, A. Hermansson,, and A. Forsgren. 1994. Protein D, the glycerophosphodiester phosphodiesterase from Haemophilus influenzae with affinity for human immunoglobulin D, influenzae virulence in a rat otitis model. Infect. Immun. 62:48484854.
21. Kaplan, M. H.,, and J. E. Volankis. 1974. Interaction of Creactive protein complexes with the complement system. I. Consumption of human complement associated with the reaction of CRP with pneumococcal C-polysaccharide and with choline phosphates, lecthin and sphingomyelin. J. Immunol. 112:21352147.
22. Kenny, J.,, G. Guelde,, R. Fischer,, and D. Longo. 1994. Induction of phosphocholine-specific antibodies in X-linked immune deficient mice: in vivo protection against a Streptococcus pneumoniae challenge. Int. Immunol. 6:561568.
23. Kilian, M.,, J. Reinholdt,, H. Lomholt,, K. Poulsen,, and E. Frandsen. 1996. Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: critical evaluation of experimental evidence. APMIS 104:321338.
24. Kim, J.,, and J. Weiser. 1998. Association of intrastrain phase variation in quantity of capsular polysaccharide and teichoic acid with the virulence of Streptococcus pneumoniae. J. Infect. Dis. 177:368377.
25. Kim, J. O.,, S. Romero-Steiner,, U. Sörensen,, J. Blom,, M. Carvalho,, S. Barnardi,, G. Carlone,, and J. N. Weiser. 1999. Relationship between cell-surface carbohydrates and intrastrain variation on opsonophagocytosis of Streptococcus pneumoniae. Infect. Immun. 67:23272333.
26. Kroes, I.,, P. Lepp,, and D. Relman. 1999. Bacterial diversity within the human subgingival crevice. Proc. Natl. Acad. Sci. USA 96:1454714552.
27. Laferriere, C. A.,, R. K. Soo,, J. M. de Muys,, F. Michon,, and H. J. Jennings. 1997. The synthesis of Streptococcus pneumoniae polysaccharide-tetanus toxoid conjugates and the effect of chain length on immunogenicity. Vaccine 15:179186.
28. Lamark, T.,, I. Kaasen,, M. W. Eshoo,, P. Falkenberg,, J. McDougall,, and A. R. Strom. 1991. DNA sequence and analysis of the bet genes encoding the osmoregulatory cholineglycine betaine pathway of Escherichia coli. Mol. Microbiol. 5:10491064.
29. Lysenko, E.,, J. Gould,, R. Bals,, J. Wilson,, and J. Weiser. 2000. Bacterial phosphorylcholine decreases susceptibility to the antimicrobial peptide LL-37/hCAP18 expressed in the upper respiratory tract. Infect. Immun. 68:16641671.
30. Lysenko, E.,, J. Richards,, A. Cox,, A. Stewart,, A. Martin,, M. Kapoor,, and J. Weiser. 2000. The position of phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae affects binding and sensitivity to C-reactive protein mediated killing. Mol. Microbiol. 35:234245.
31. Mi, Q.,, L. Zhou,, D. Schulze,, R. Fischer,, A. Lustig,, L. Rezanka,, D. Donovan,, D. Longo,, and J. Kenny. 2000. Highly reduced protection against Streptococcus pneumoniae after deletion of a single heavy chain gene in mouse. Proc. Natl. Acad. Sci. USA 97:60316036.
32. Moser, C.,, D. Weiner,, E. Lysenko,, R. Bals,, J. Weiser,, and J. Wilson. 2002. ?-Defensin 1 contributes to pulmonary innate immunity in mice. Infect. Immun. 70:30683072.
33. Moxon, E.,, R. Lenski,, and P. Rainey. 1998. Adaptive evolution of highly mutable loci in pathogenic bacteria. Perspect. Biol. Med. 42:154155.
34. Moxon, E. R.,, and C. Wills. 1999. DNA microsatellites: agents of evolution? Sci. Am. 280:9499.
35. Munson, R. S. J.,, and K. Sasaki. 1993. Protein D, a putative immunoglobulin D-binding protein produced by Haemophilus influenzae, is a glycerophosphodiester phophodiesterase. Infect. Immun. 175:45694571.
36. Musher, D. M.,, A. J. Chapman,, A. Goree,, S. Jonsson,, D. Briles,, and R. E. Baughn. 1986. Natural and vaccine-related immunity to Streptococcus pneumoniae. J. Infect. Dis. 154:245256.
37. Nordenstam, G.,, B. Andersson,, D. Briles,, J. W. J. Brooks,, A. Oden,, A. Svanborg,, and C. S. Eden. 1990. High anti-phosphorylcholine antibody levels and mortality associated with pneumonia. Scand. J. Infect. Dis. 22:187195.
38. Purkall, D.,, J. Tew,, and H. Schenkein. 2002. Opsonization of Actinobacillus actinomycetemcomitans by immunoglobulin G antibody reactive with phosphorylcholine. Infect. Immun. 70: 64856488.
39. Rao, V.,, G. Krasan,, D. Hendrixson,, S. Dawid,, and J. W. St. Geme III. 1999. Molecular determinants of the pathogenesis of disease due to non-typable Haemophilus influenzae. FEMS Microbiol. Rev. 23:99129.
40. Ring, A.,, J. N. Weiser,, and E. I. Tuomanen. 1998. Pneumococcal penetration of the blood-brain barrier: molecular analysis of a novel re-entry path. J. Clin. Investig. 102:347360.
41. Schenkein, H.,, S. Barbour,, C. Berry,, B. Kipps,, and J. Tew. 2000. Invasion of human vascular endothelial cells by Actinobacillus actinomycetemcomitans via the receptor for platelet-activating factor. Infect. Immun. 68:54165419.
42. Schweda, E.,, J. Li,, E. Moxon,, and J. Richards. 2002. Structural analysis of lipopolysaccharide oligosaccharide epitopes expressed by non-typeable Haemophilus influenzae strain 176. Carbohydr. Res. 337:409420.
43. Schweda, E. K. H.,, H. Masoud,, A. Martin,, A. Risberg,, D. W. Hood,, E. R. Moxon,, J. N. Weiser,, and J. C. Richards. 1997. Phase variable expression and characterization of phosphorylcholine oligosaccharide epitopes in Haemophilus influenzae lipopolysaccharides. Glycoconj. J. 14:S23.
44. Scott, M. G.,, D. E. Briles,, P. G. Shackelford,, D. S. Smith,, and M. H. Nahm. 1987. Human antibodies to phosphocholine. IgG anti-PC antibodies express restricted numbers of V and C regions. J. Immunol. 138:33253331.
45. Serino, L.,, and M. Virji. 2002. Genetic and functional analysis of the phosphorylcholine moiety of commensal Neisseria lipopolysaccharide. Mol. Microbiol. 43:437448.
46. Serino, L.,, and M. Virji. 2000. Phosphorylcholine decoration of lipopolysaccharide differentiates commensal neisseriae from pathogenic strains: identification of licA-type genes in commensal neisseriae. Mol. Microbiol. 35:15501559.
47. Sohlenkamp, C.,, I. Lopez-Lara,, and O. Geiger. 2003. Biosynthesis of phosphatidylcholine in bacteria. Prog. Lipid Res. 42: 115162.
48. Sorenson, U. B. S.,, J. Henrichsen,, H.-C. Chen,, and S. C. Szu. 1990. Covalent linkage between the capsular polysaccharide and cell wall peptidoglycan of Streptococcus pneumoniae revealed by immunochemical methods. Microb. Pathog. 8:325334.
49. Swords, W.,, B. Buscher,, K. Ver Steeg Ii,, A. Preston,, W. Nichols,, J. Weiser,, B. Gibson,, and M. Apicella. 2000. Nontypeable Haemophilus influenzae adhere to and invade human bronchial epithelial cells via an interaction of lipooligosaccharide with the PAF receptor. Mol. Microbiol. 37:1327.
50. Szalai, A.,, J. VanCott,, J. McGhee,, J. Volanakis,, and W. J. Benjamin. 2000. Human C-reactive protein is protective against fatal Salmonella enterica serovar Typhimurium infection in transgenic mice. Infect. Immun. 68:56525656.
51. Szalai, A. J.,, A. Agrawal,, T. J. Greenhough,, and J. E. Volanakis. 1997. C-reactive protein. Immunol. Res. 16:127136.
52. Szalai, A. J.,, D. E. Briles,, and J. E. Volanakis. 1995. Human C-reactive protein is protective against fatal Streptococcus pneumoniae infection in transgenic mice. J. Immunol. 155: 25572563.
53. Szu, S.,, R. Schneerson,, and J. Robbins. 1986. Rabbit antibodies to the cell wall polysaccharide of Streptococcus pneumoniae fail to protect mice from lethal challenge with encapsulated pneumococci. Infect. Immun. 54:448455.
54. Thomas, A. M.,, P. A. Lambert,, and I. R. Poxton. 1978. The uptake of choline by Streptococcus pneumoniae. J. Gen. Microbiol. 109:313317.
55. Warren, M. J.,, and M. P. Jennings. 2003. Identification and characterization of pptA: a gene involved in the phase-variable expression of phosphorylcholine on pili of Neisseria meningitidis. Infect. Immun. 71:68926898.
56. Weiser, J.,, D. Bae,, H. Epino,, S. Gordon,, M. Kapoor,, L. Zenewicz,, and M. Shchepetov. 2001. Changes in availability of oxygen accentuate differences in capsular polysaccharide expression by phenotypic variants and clinical isolates of Streptococcus pneumoniae. Infect. Immun. 69:54305439.
57. Weiser, J.,, D. Bae,, C. Fasching,, R. Scamurra,, A. Ratner,, and E. Janoff. 2003. Antibody-enhanced pneumococcal adherence requires IgA1 protease. Proc. Natl. Acad. Sci. USA 100:415420.
58. Weiser, J.,, and E. Tuomanen. 2002. A disease-oriented approach to the discovery of novel vaccines, p. 139-148. In B. Bloom and P.-H. Lambert (ed.), The Vaccine Book. Academic Press, Inc., New York, N.Y..
59. Weiser, J. N., 1999. Phase-variation of Streptococcus pneumoniae, p. 225231. In V. Fischetti (ed.), Gram-Positive Pathogens. ASM Press, Washington, D.C..
60. Weiser, J. N.,, R. Austrian,, P. K. Sreenivasan,, and H. R. Masure. 1994. Phase variation in pneumococcal opacity: relationship between colonial morphology and nasopharyngeal colonization. Infect. Immun. 62:25822589.
61. Weiser, J. N.,, J. B. Goldberg,, N. Pan,, L. Wilson,, and M. Virji. 1998. The phosphorylcholine epitope undergoes phase variation on a 43-kDa protein in Pseudomonas aeruginosa and on pili of pathogenic Neisseria. Infect. Immun. 66: 42634267.
62. Weiser, J. N.,, J. M. Love,, and E. R. Moxon. 1989. The molecular mechanism of phase variation of H. influenzae lipopolysaccharide. Cell 59:657665.
63. Weiser, J. N.,, D. J. Maskell,, P. D. Butler,, A. A. Lindberg,, and E. R. Moxon. 1990. Characterization of repetitive sequences controlling phase variation of Haemophilus influenzae lipopolysaccharide. J. Bacteriol. 172:33043309.
64. Weiser, J. N.,, N. Pan,, K. L. McGowan,, D. Musher,, A. Martin,, and J. C. Richards. 1998. Phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae contributes to persistence in the respiratory tract and sensitivity to serum killing mediated by C-reactive protein. J. Exp. Med. 187:631640.
65. Weiser, J. N.,, M. Shchepetov,, and S. T. H. Chong. 1997. Decoration of lipopolysaccaride with phosphorylcholine: a phase-variable characteristic of Haemophilus influenzae. Infect. Immun. 65:943950.
66. Wilderman, P.,, A. Vasil,, W. Martin,, R. Murphy,, and M. Vasil. 2002. Pseudomonas aeruginosa synthesizes phosphatidylcholine by use of the phosphatidylcholine synthase pathway. J. Bacteriol. 184:47924799.
67. Wilson, E.,, M. Deehan,, E. Katz,, K. Brown,, K. Houston,, J. O’Grady,, M. Harnett,, and W. Harnett. 2003. Hyporesponsiveness of murine B lymphocytes exposed to the filarial nematode secreted product ES-62 in vivo. Immunology 109:238245.
68. Yee, A.,, H. Phan,, R. Zuniga,, J. Salmon,, and D. Musher. 2000. Association between FcgammaRIIa-R131 allotype and bacteremic pneumococcal pneumonia. Clin. Infect. Dis. 30: 2528.
69. Yother, J.,, K. Leopold,, J. White,, and W. Fischer. 1998. Generation and properties of a Streptococcus pneumoniae mutant which does not require choline or analogs for growth. J. Bacteriol. 180:20932101.
70. Zhang, J.-R.,, I. Idanpaan-Heikkila,, W. Fischer,, and E. Tuomanen. 1999. Pneumococcal licD2 gene is involved in phosphorylcholine metabolism. Mol. Microbiol. 31:14771488.

Tables

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Table 1

Bacteria expressing the ChoP antigen/structure

Citation: Weiser J. 2005. Role of Phosphorylcholine in Respiratory Tract Colonization, p 61-72. In Nataro J, Cohen P, Mobley H, Weiser J (ed), Colonization of Mucosal Surfaces. ASM Press, Washington, DC. doi: 10.1128/9781555817619.ch5

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