Role of Antibody-Mediated Immunity in Host Defense against Mycobacterium tuberculosis

Aharona Glatman-Freedman; Arturo Casadevall

doi:10.1128/9781555817657.ch32

Chapter 32 : Role of Antibody-Mediated Immunity in Host Defense against Mycobacterium tuberculosis

Authors: Aharona Glatman-Freedman¹, Arturo Casadevall²

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Affiliations: 1: Division of Infectious Diseases, Department of Pediatrics, Childrenapos;s Hospital at Montefiore, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461; 2: Division of Infectious Diseases, Departments of Medicine and of Microbiology and Immunology, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461

Content Type: Monograph

Publication Year: 2005

Category: Bacterial Pathogenesis; Clinical Microbiology

Book DOI: 10.1128/9781555817657

Chapter DOI: 10.1128/9781555817657.ch32

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Abstract:

For many decades, the dominant view in the field of mycobacterial immunology has been that host defense against Mycobacterium tuberculosis relies exclusively on cell-mediated immunity. In search of new solutions to the overwhelming problem of tuberculosis, investigators set out several years ago to evaluate the help that can be offered by antibody-mediated immunity in host defense against M. tuberculosis, with the possibility that it may lead to the development of a novel and effective vaccine strategy. The literature on studies of antibody-mediated immunity against M. tuberculosis can be divided into several general categories: serological studies, passive antibody studies, animal studies, in vitro studies, and human studies. Monoclonal antibody (MAb) technology, described for the first time in the 1970s, allowed the selection of individual antibodies with particular antigen specificities. Vaccines presently used in humans belong to one of three main categories: inactivated, live attenuated, and subunit vaccines. Adhesion of microbes to host tissues is a significant step in the colonization of the host and the establishment of infection. The majority of these vaccines are thought to provide protection by eliciting protective antibody responses. The progress made in recent years is encouraging and should stimulate interest in evaluating the mechanisms by which antibodies may contribute to host defense against M. tuberculosis. The future challenges are to systematically dissect the conditions required for optimal antibody-mediated immunity against M. tuberculosis and to develop vaccine candidates that will work by eliciting protective antibody responses.

Citation: Glatman-Freedman A, Casadevall A. 2005. Role of Antibody-Mediated Immunity in Host Defense against Mycobacterium tuberculosis, p 497-512. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch32

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Role of Antibody-Mediated Immunity in Host Defense against Mycobacterium tuberculosis

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Figure 1

Schematic representation of a proposed mechanism for antibody-mediated immunity to M. tuberculosis. 1, Interference with adhesion to macrophages (1a) or respiratory epithelium (1b); 2, neutralization or clearance of mycobacterial antigens or toxins; 3, promotion of phagosome-lysosome fusion; 4, opsonization via Fc receptor; 5, complement activation; 6, effect on signal transduction with release of cytokines and chemokines.

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Figure 1

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Figure 2

Survival (A) and body weight (B) of C57BL/6 mice immunized with AM conjugated to tetanus toxoid (TT) in L3 adjuvant emulsion (top panels) or suspension (middle panels), as compared to mice immunized with BCG (bottom panels) and infected intranasally with M. tuberculosis (105 CFU). Black symbols represent mice immunized with AM conjugate vaccine or BCG, and open symbols represent controls. Adapted from reference 36. © 2003 with permission from Elsevier.

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References

/content/book/10.1128/9781555817657.chap32

1. Andersen, P. 1997. Host responses and antigens involved in protective immunity to Mycobcterium tuberculosis. Scand. J. Immunol. 45: 115– 131.

2. Armstrong, J. A.,, and P. D. Hart. 1975. Phagosome-lysosome interactions in cultured macrophages infected with virulent tubercle bacilli. J. Exp. Med. 142: 1– 16.

3. Band, H.,, S. Sinha,, and G. P. Talwar. 1987. Inhibition of interaction of mycobacteria with Schwann cells by antimycobacterial antibodies. J. Neuroimmunol. 14: 235– 239.

4. Barrera, L.,, I. de Kantor,, V. Ritacco,, A. Reniero,, B. Lopez,, J. Benetucci,, M. Beltran,, O. Libonatti,, E. Padula,, J. Castagnino,, and L. Gonzalez Montaner. 1992. Humoral response to Mycobacterium tuberculosis in patients with human immunodeficiency virus infection. Tubercle Lung Dis. 73: 187– 191.

5. Bluhm, I. 1952. The influence of immune and normal human serum on the respiration of tubercle bacilli. Acta Med. Scand. Suppl. 275: 1– 28.

6. Bosio, C. M.,, D. Gardner,, and K. L. Elkins. 2003. Infection of B cell-deficient mice with CDC 1551, a clinical isolate of Mycobacterium tuberculosis: delay in dissemination and development of lung pathology. J. Immunol. 164: 6417– 6425.

7. Buttery, J.,, and E. R. Moxon. 2002. Capsulate bacteria and the lung. Br. Med. Bull. 61: 63– 80.

8. Calmette, A. 1923. Passive immunity: attempts at antituberculous serotherapy, p. 603– 623. In Tubercle Bacillus Infection and Tuberculosis in Man and Animals. The Williams & Wilkins Co., Baltimore, Md.

9. Casadevall, A. 2003. Antibody-mediated immunity against intracellular pathogens: two-dimentional thinking comes full circle. Infect. Immun. 71: 4225– 4228.

10. Casadevall, A.,, and M. D. Scharff. 1994. Serum therapy revisited: animal models of infection and development of passive antibody therapy. Antimicrob. Agents Chemother. 38: 1695– 1702.

11. Casadevall, A.,, and M. D. Scharff. 1995. Return to the past: the case for antibody-based therapies in infectious diseases. Clin. Infect. Dis. 21: 150– 161.

12. Centers for Disease Control and Prevention. 1996. The role of BCG vaccine in the prevention and control of tuberculosis in the United States. A joint statement by the Advisory Council for the Elimination of Tuberculosis and the Advisory Committee on Immunization Practices. Morb. Mortal. Wkly. Rep. 45: 1– 18.

12.a. Chambers, M. A.,, D. Gavier-Widén,, and R. G. Hewinson. 2004. Antibody bound to the surface antigen MPB83 of Mycobacterium bovis enhances survival against high dose and low dose challenge. FEMS Immunol. Med. Microbiol. 41: 93– 100.

13. Chan, J.,, and S. H. E. Kaufmann,. 1994. Immune mechanism of protection, p. 389– 415. In B. R. Barry (ed.), Tuberculosis. Pathogenesis, Protection, and Control. ASM Press, Washington, D.C.

14. Chatterjee, D.,, K. Lowell,, B. Rivoire,, M. R. McNeil,, and P. J. Brennan. 1992. Lipoarabinomannan of Mycobacterium tuberculosis. Capping with mannosyl residues in some strains. J. Biol. Chem. 267: 6234– 6239.

15. Choucroun, N. 1949. Precipitin test for carbohydrate antibodies in human tuberculosis. Am. Rev. Tuberc. 59: 710– 712.

16. Choudhury, A.,, N. F. Mistry,, and N. H. Antia. 1989. Blocking of Mycobacterium leprae adherence to dissociated Schwann cells by anti-mycobacterial antibodies. Scand. J. Immunol. 30: 505– 509.

17. Clawson, B. J. 1936. The destruction of tubercle bacilli within phagocytes in vitro. J. Infect. Dis. 58: 64– 69.

18. Collins, F. M. 1991. Antituberculous immunity: new solutions to an old problem. Rev. Infect. Dis. 13: 940– 950.

19. Collins, H. L.,, and S. H. E. Kaufmann. 2001. Prospects for better tuberculosis vaccines. Lancet Infect. Dis. 1: 21– 28.

20. Conti, S.,, F. Fanti,, W. Magliani,, M. Gerloni,, D. Bertolotti,, A. Salati,, A. Cassone,, and L. Polonelli. 1998. Mycobactericidal activity of human natural, monoclonal, and recombinant yeast killer toxin-like antibodies. J. Infect. Dis. 177: 807– 811.

21. Costello, A. M.,, A. Kumar,, V. Narayan,, M. S. Akbar,, S. Ahmed,, C. Abou-Zeid,, G. A. W. Rook,, J. Stanford,, and C. Moreno. 1992. Does antibody to mycobacterial antigens, including lipoarabinomannan, limit dissemination in childhood tuberculosis? Trans. R. Soc. Trop. Med. Hyg. 86: 686– 692.

22. Da Costa, C. T. K. A.,, S. Khanolkar-Young,, A. M. Elliott,, K. M. A. Wasunna,, and K. P. W. J. McAdam. 1993. Immunoglobulin G subclass responses to mycobacterial lipoarabinomannan in HIV-infected and non-infected patients with tuberculosis. Clin. Exp. Immunol. 91: 25– 29.

23. Daffe, M.,, and P. Draper. 1998. The envelope layers of mycobacteria with reference to their pathogenicity. Adv. Microb. Physiol. 39: 131– 203.

24. Daniel, T. M.,, M. J. Oxtoby,, E. M. Pinto,, and E. S. Moreno. 1981. The immune spectrum in patients with pulmonary tuberculosis. Am. Rev. Respir. Dis. 123: 556– 559.

25. De Schweinitz, E. A., and M. Dorset. 1897. Some products of the tuberculosis bacillus and the treatment of experimental tuberculosis with antitoxic serum. N. Y. Med. J. 66: 105– 111.

26. Dunlap, N. E.,, and D. E. Briles. 1993. Immunology of tuberculosis. Med. Clin. North Am. 77: 1235– 1251.

27. Emmart, E. W.,, and F. B. Seibert. 1945. The effect of tuberculous and sensitized sera and serum fractions on the development of tubercles in the chorio-allantoic membrane of the chick. J. Immunol. 50: 143– 160.

28. Engele, M.,, E. Stossel,, K. Castiglione,, N. Schwerdtner,, M. Wagner,, P. Bolcskei,, M. Rollinghoff,, and S. Stenger. 2002. Induction of TNF in human alveolar macrophages as a potential evasion mechanism of virulent Mycobacterium tuberculosis. J. Immunol. 168: 1328– 1337.

29. Falero-Diaz, G.,, S. Challacombe,, D. Rahman,, M. Mistry,, G. Douce,, G. Dougan,, A. Acosta,, and J. Ivanyi. 2000. Transmission of IgA and IgG monoclonal antibodies to mucosal fluids following intranasal or parenteral delivery. Int. Arch. Allergy Immunol. 122: 143– 150.

30. Feldmesser, M.,, and A. Casadevall. 1997. Effect of serum IgG1 to Cryptococcus neoformans glucuronoxylomannan on murine pulmonary infection. J. Immunol. 158: 790– 799.

31. Fisch, C. 1897. The antitoxic and bactericidal properties of the serum of horses treated with Koch’s new tuberculin. JAMA 29: 882– 889.

32. Forget, A.,, J. C. Benoit,, R. Turcotte,, and N. Gusew-Chartrand. 1976. Enhancement activity of anti-mycobacterial sera in experimental Mycobacterium bovis (BCG) infection in mice. Infect. Immun. 13: 1301– 1306.

33. Glatman-Freedman, A. 2003. Advances in antibody-mediated immunity against Mycobacterium tuberculosis: implications for a novel vaccine strategy. FEMS Immunol. Med. Microbiol. 39: 9– 16.

34. Glatman-Freedman, A.,, and A. Casadevall. 1998. Serum therapy for tuberculosis revisited: reappraisal of the role of antibody-mediated immunity against Mycobacterium tuberculosis. Clin. Microbiol. Rev. 11: 514– 532.

34.a. Glatman-Freedman, A.,, A. Casadevall,, Z. Dai,, W. R. Jacobs, Jr.,, A. Li,, S. L. Morris,, J. A. Navoa,, S. Piperdi,, J. B. Robbins,, R. Schneerson,, J. R. Schwebach,, and M. Shapiro. 2004. Antigenic evidence of prevalence and diversity of Mycobacterium tuberculosis arabinomannan. J. Clin. Microbiol. 42: 3225– 3231.

35. Glatman-Freedman, A.,, A. J. Mednick,, N. Lendvai,, and A. Casadevall. 2000. Clearance and organ distribution of Mycobacterium tuberculosis lipoarabinomannan (LAM) in the presence and absence of LAM-binding IgM. Infect. Immun. 68: 335– 341.

36. Hamasur, B.,, M. Haile,, A. Pawlowski,, U. Schroder,, A. Williams,, G. Hatch,, G. Hall,, P. Marsh,, G. Kallenius,, and S. B. Svenson. 2003. Mycobacterium tuberculosis arabinomannan- protein conjugates protect against tuberculosis. Vaccine 21: 4081– 4093.

37. Hamasur, B.,, G. Kallenius,, and S. B. Svenson. 1999. Synthesis and immunologic characterization of Mycobacterium tuberculosis lipoarabinomannan specific oligosaccharideprotein conjugates. Vaccine 17: 2853– 2861.

38. Hayden, A. M. 1896. Report of results and recoveries obtained by the use of anti-tubercle serum. JAMA 26: 965– 966.

39. Hetland, G.,, H. G. Wiker,, K. Hogasen,, B. Hamasur,, S. B. Svenson,, and M. Harboe. 1998. Involvement of antilipoarabinomannan antibodies in classical complement activation in tuberculosis. Clin. Diagn. Lab. Immunol. 5: 211– 218.

40. Holmes, A. M. 1899. A further report on the use of “antiphthisic serum T.R.” (Fisch) in tuberculosis. JAMA 33: 886– 888.

41. Hussain, R.,, H. Shiratsuchi,, J. J. Ellner,, and R. S. Wallis. 2000. PPD-specific IgG1 antibody subclass upregulate tumor necrosis factor expression in PPD-stimulated monocytes: possible link with disease pathogenesis in tuberculosis. Clin. Exp. Immunol. 119: 449– 455.

42. Hussain, R.,, H. Shiratsuchi,, M. Phillips,, J. J. Ellner,, and R. S. Wallis. 2001. Opsonizing antibodies (IgG1) upregulate monocyte proinflammatory cytokines tumour necrosis factor-alpha (TNF-α) and IL-6 but not anti-inflammatory cytokine IL-10 in mycobacterial antigen-stimulated monocytes implications for pathogenesis. Clin. Exp. Immunol. 123: 210– 218.

43. Johnson, C. M.,, A. M. Cooper,, A. A. Frank,, C. B. C. Bonorino,, L. J. Wysoki,, and I. M. Orme. 1997. Mycobacterium tuberculosis aerogenic rechallenge infections in B celldeficient mice. Tubercle Lung. Dis. 78: 257– 261.

44. Josset, A. 1924. Les conditions de succes de la serotherapie antituberculeuse chez l’homme. Bull. Mem. Soc. Medi. Hop. Paris 40: 923– 939.

45. Josset, A. 1924. Seize année de serotherapie antituberculeuse. Bull. Mem. Soc. Med. Hop. Paris 40: 777– 781.

46. Josset, A. 1924. Resultats experimentaux de la serotherapie antituberculeuse. Bull. Mem. Soc. Hop. Paris 40: 826– 831.

47. Kardito, T.,, and J. M. Grange. 1980. Immunological and clinical features of smear-positive pulmonary tuberculosis in East Java. Tubercle 61: 231– 238.

48. Kato, M. 1972. Antibody formation to trehalose-6,6'-dimycolate (cord factor) of Mycobacterium tuberculosis. Infect. Immun. 5: 203– 212.

49. Kato, M. 1974. Further study on neutralization of biochemical activity of cord factor by anti-cord factor antibody. Infect. Immun. 10: 277– 279.

50. Kisich, K. O.,, M. Higgins,, G. Diamond,, and L. Heifets. 2002. Tumor necrosis factor alpha stimulates killing of Mycobacterium tuberculosis by human neutrophils. Infect. Immun. 70: 4591– 4599.

51. Lemen, J. R. 1898. Three years of serum therapy in tuberculosis. N. Y. Med. J. 67: 672– 677.

52. Lenzini, L.,, P. Rottoli,, and L. Rottoli. 1977. The spectrum of human tuberculosis. Clin. Exp. Immunol. 27: 230– 237.

53. Lesinski, G. B., and M. A. Westerink. 2001. Vaccines against polysaccharide antigens. Curr. Drug Targets Infect. Disorders 1: 325– 334.

54. Macpherson, A. J. S.,, A. Lamarre,, K. McCoy,, G. R. Harriman,, B. Odermatt,, G. Dougan,, H. Hengartner,, and R. M. Zinkernagel. 2001. IgA production without mu or delta chain expression in developing B cells. Nat. Immunol. 2: 625– 631.

55. Maragliano, C. 1896. Le serum antituberculeux et son antitoxine. Rev. Tuberc. 1896: 131– 138.

56. Maragliano, E. 1896. Premiere statistique du traitement de la tuberculose par la serum Maragliano. Rev. Tuberc. 1896: 156– 157.

57. Marchant, C. D., and M. L. Kumar,. 2002. Immunizations, p. 232– 262. In H. B. Jenson, and R. S. Baltimore (ed.), Pediatric Infectious Diseases: Principles and Practices. The W. B. Saunders Co., Philadelphia, Pa.

58. Marmorek, A. 1903. Antituberculous serum and “vaccine.” Lancet ii: 1642– 1645.

59. Menozzi, F. D.,, J. H. Rouse,, M. Alavi,, M. Laude-Sharp,, J. Muller,, R. Bischoff,, M. J. Brennan,, and C. Locht. 1996. Identification of a heparin-binding hemagglutinin present in mycobacteria. J. Exp. Med. 184: 993– 1001.

60. Michell, S. L.,, A. O. Whelan,, P. R. Wheeler,, M. Panico,, R. L. Easton,, A. T. Etienne,, S. M. Haslam,, A. Dell,, H. R. Morris,, A. J. Reason,, J. L. Herrmann,, D. B. Young,, and R. G. Hewinson. 2003. The MPB83 antigen from Mycobacteium bovis contains O-linked mannose and (1→3) mannobiose moieties. J. Biol. Chem. 278: 16423– 16432.

61. Mukherjee, J.,, G. Nussbaum,, M. D. Scharff,, and A. Casadevall. 1995. Protective and nonprotective monoclonal antibodies to Cryptococcus neoformans originating from one B cell. J. Exp. Med. 181: 405– 409.

62. Mukherjee, J.,, M. D. Scharff,, and A. Casadevall. 1992. Protective murine monoclonal antibodies to Cryptococcus neoformans. Infect. Immun. 60: 4534– 4541.

63. Mukherjee, S.,, S. C. Lee,, and A. Casadevall. 1995. Antibodies to Cryptococcus neoformans glucuronoxylomannan enhance antifungal activity of murine macrophages. Infect. Immun. 63: 573– 579.

64. Nigou, J.,, M. Gilleron,, M. Rojas,, L. F. Garcia,, M. Thurnher,, and G. Puzo. 2002. Mycobacterial lipoarabinomannans: modulators of dendritic cell function and the apoptotic response. Microbes Infect. 4: 945– 953.

65. Nussbaum, G.,, W. Cleare,, A. Casadevall,, M. D. Scharff,, and P. Valdom. 1997. Epitope location in the Cryptococcus neoformans capsule is a determinant of antibody efficacy. J. Exp. Med. 185: 685– 694.

66. Nussbaum, G.,, R. Yuan,, A. Casadevall,, and M. D. Scharff. 1996. Immunoglobulin G3 blocking antibodies to the fungal pathogen Cryptococcus neoformans. J. Exp. Med. 183: 1905– 1909.

67. Paquin, P. 1895. The treatment of tuberculosis by injections of immunized blood serum. JAMA 24: 842– 845.

68. Paquin, P. 1895. Anti tubercle serum. JAMA 24: 341– 346.

69. Paquin, P. 1897. Further report of cases treated with antitubercle serum. JAMA 29: 98– 99.

70. Paquin, P. 1898. How we treat consumption today. JAMA 30: 294– 299.

71. Peterson, J. C.,, R. Langercranz,, S. I. Rollof,, and J. Lind. 1952. Tuberculin hemmagglutination studies in active tuberculosis infections, benign and virulent. Acta Paediatr. 41: 57– 73.

72. Pethe, K.,, S. Alonso,, F. Biet,, G. Delogu,, M. J. Brennan,, C. Locht,, and F. D. Menozzi. 2001. The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination. Nature 412: 190– 194.

73. Prioleau, W. H. 1898. Antitubercle serum (Paquin) in tuberculosis. JAMA 31: 687– 688.

74. Raffel, S. 1946. The relationship of acquired resistance, allergy, antibodies and tissue reactivities to the components of the tubercle bacillus. Am. Rev. Tuberc. 54: 564– 573.

75. Reggiardo, Z.,, and G. Middlebrook. 1974. Failure of passive serum transfer of immunity against aerogenic tuberculosis in rabbits. Proc. Soc. Exp. Biol. Med. 145: 173– 175.

76. Reiss, F.,, G. Szilagyi,, and E. Mayer. 1975. Immunological studies of anticryptococcal factor of normal human serum. Mycopathologia 55: 175– 178.

77. Roach, D. R.,, A. G. Bean,, C. Demangel,, M. P. France,, H. Briscoe,, and W. J. Britton. 2002. TNF regulates chemokine induction essential for cell recruitment, granuloma formation, and clearance of mycobacterial infection. J. Immunol. 168: 4620– 4627.

78. Robbins, J. B.,, R. Schneerson,, and S. C. Szu. 1996. Hypothesis: how licenced vaccines confer protective immunity. Adv. Exp. Med. Biol. 397: 169– 182.

79. Ryll, R.,, Y. Kumazawa,, and I. Yano. 2001. Immunological properties of trehalose dimycolate (cord factor) and other mycolic acid-containing glycolipids—a review. Microbiol. Immunol. 45: 801– 811.

80. Sanchez-Rodriguez, C.,, C. Estrada-Chavez,, J. Garcia-Vigil,, F. Laredo-Sanchez,, J. Halabe-Cherem,, A. Pereira-Suarez,, and R. Mancilla. 2002. An IgG antibody response to the antigen 85 complex is associated with good outcome in Mexican Totonaca Indians with pulmonary tuberculosis. Int. J. Tuberc. Lung Dis. 6: 706– 712.

81. Sanford, J. E.,, D. M. Lupan,, A. M. Schlageter,, and T. R. Kozel. 1990. Passive immunization against Cryptococcus neoformans with an isotype-switch family of monoclonal antibodies reactive with cryptococcal polysaccharide. Infect. Immun. 58: 1919– 1923.

82. Schlesinger, L. S. 1998. Mycobacterium tuberculosis and the complement system. Trends Microbiol. 6: 47– 49.

83. Schlesinger, L. S.,, and M. A. Horwitz. 1991. Phenolic glycolipid-1 of Mycobacterium leprae binds complement component C3 in serum and mediates phagocytosis by human monocytes. J. Exp. Med. 174: 1031– 1038.

84. Schlesinger, L. S.,, S. R. Hull,, and T. M. Kaufman. 1994. Binding of the terminal mannosyl units of lipoarabinomannan from a virulent strain of Mycobacterium tuberculosis to human macrophages. J. Immunol. 152: 4070– 4079.

85. Schwebach, J. R.,, A. Casadevall,, R. Schneerson,, Z. Dai,, X. Wang,, J. B. Robbins,, and A. Glatman-Freedman. 2001. Expression of a Mycobacterium tuberculosis arabinomannan antigen in vitro and in vivo. Infect. Immun. 69: 5671– 5678.

86. Schwebach, J. R.,, A. Glatman-Freedman,, L. Gunter-Cummins,, Z. Dai,, J. R. Robbins,, R. Schneerson,, and A. Casadevall. 2002. Glucan is a component of the Mycobacterium tuberculosis surface that is expressed in vitro and in vivo. Infect. Immun. 70: 2566– 2575.

87. Seibert, F. B. 1956. The significance of antigen-antibody reactions in tuberculosis. J. Infect. Dis. 99: 76– 83.

88. Seibert, F. B. 1958. The interplay of an immune substance with tuberculopolysaccharide and its antibody in tuberculosis. J. Infect. Dis. 103: 52– 60.

89. Seibert, F. B.,, E. E. Miller,, U. Buseman,, M. V. Seibert,, E. Soto-Figueroa,, and L. Fry. 1956. The significance of antibodies to tuberculoprotein and polysaccharide in resistance to tuberculosis. Am. Rev. Tuberc. Pulm. Dis. 73: 547– 562.

90. Seibert, F. B.,, and J. W. Nelson. 1943. Proteins of tuberculin. J. Am. Chem. Soc. 65: 272– 278.

91. Seibert, F. B.,, and M. V. Seibert. 1957. Relationship between immunity and circulating antibodies, complement and tuberculopolysaccharide in tuberculosis. J. Infect. Dis. 101: 109– 118.

92. Shropshire, L. L. 1896. A limited experience with the Paul Paquin antitubercle serum. N. Y. Med. J. 63: 15– 16.

93. Smith, S.,, D. Liggitt,, E. Jeromsky,, X. Tan,, S. J. Skerrett,, and C. B. Wilson. 2002. Local role for tumor necrosis factor alpha in the pulmonary inflammatory response to Mycobacterium tuberculosis infection. Infect. Immun. 70: 2082– 2089.

94. Snider, D. E.,, M. Raviglione,, and A. Kochi,. 1994. Global burden of tuberculosis, p. 3– 11. In B. R. Bloom (ed.), Tuberculosis. Pathogenesis, Protection, and Control. ASM Press, Washington, D.C.

95. Spahlinger, H. 1922. Note on the treatment of tuberculosis. Lancet i: 5– 8.

96. Strohmeier, G. R.,, and M. J. Fenton. 1999. Roles of lipoarabinomannan in the pathogenesis of tuberculosis. Microbes Infect. 1: 709– 717.

97. Stubbert, J. E. 1898. Some statistics upon sero-therapy in tuberculosis. Trans. Am. Climatol. Assoc. 14: 214– 230.

98. Teitelbaum, R.,, A. Glatman-Freedman,, B. Chen,, J. B. Robbins,, E. Unanue,, A. Casadevall,, and B. R. Bloom. 1998. A mAb recognizing a surface antigen of Mycobacterium tuberculosis enhances host survival. Proc. Natl. Acad. Sci. USA 95: 15688– 15693.

99. Trotter, C. L.,, M. E. Ramsay,, and E. B. Kaczmarski. 2002. Meningococal serogroup C conjugate vaccination in England and Wales: coverage and initial impact of the campaign. Commun. Dis. Public Health 5: 220– 225.

100. Trudeau, E. L.,, and E. R. Baldwin. 1898. Experimental studies on the preparation and effects of antitoxins for tuberculosis. Am. J. Med. Sci. 116: 692– 707.

101. Trudeau, E. L.,, and E. R. Baldwin. 1899. Experimental studies on the preparation and effects of antitoxins for tuberculosis. Am. J. Med. Sc. 117: 56– 76.

102. Tsuji, S.,, K. Ito,, and S. Oshima. 1957. The role of humoral factors in native and acquired resistance to tuberculosis. Am. Rev. Tuberc. Pulm. Dis. 76: 90– 102.

103. Vallee, H. 1909. Sur le proprietes du serum du cheval hyperimmunise contre la tuberculose a l’aide de bacilles humains virulents. C. R. Hebd. Seances Soc. Biol. 67: 700– 702.

104. Venisse, A.,, J. J. Fournie,, and G. Puzo. 1995. Mannosylated lipoarabinomannan interacts with phagocytes. Eur. J. Biochem. 231: 440– 447.

105. Vordermeier, H. M.,, N. Venkataprasad,, D. P. Harris,, and J. Ivanyi. 1996. Increase of tuberculous infection in the organs of B cell-deficient mice. Clin. Exp. Immunol. 106: 312– 316.

106. Wiker, H. G.,, K. P. Lyashchenko,, A. M. Aksoy,, K. A. Lightbody,, J. M. Pollock,, S. V. Komissarenko,, S. O. Bobrovnik,, I. N. Kolesnikova,, L. O. Mykhalsky,, M. L. Gennaro,, and M. Harboe. 1998. Immunochemical characterization of the MPB70/80 and MPB83 proteins of Mycobacterium bovis. Infect. Immun. 66: 1445– 1452.

107. Wiker, H. G.,, S. Nagai,, R. G. Hewinson,, W. P. Russell,, and M. Harboe. 1996. Heterogenenous Expression of related MBP 70 and MPB 83 proteins distinguish various substrains of Mycobacterium bovis BCG and Mycobacterium tuberculosis H37Rv. Scand. J. Immunol. 43: 374– 380.

107.a. Williams, A.,, R. Reljic,, I. Naylor,, S. O. Clark,, G. Falero- Diaz,, M. Singh,, S. Challacombe,, P. O. Marsh,, and J. Ivanyi. 2004. Passive protection with immunoglobulin A antibodies against tuberculous early infection of the lung. Immunology 111: 328– 333.

108. Yuan, R.,, A. Casadevall,, G. Spira,, and M. D. Scharff. 1995. Isotype switching from IgG3 to IgG1 converts a nonprotective murine antibody to Cryptococcus neoformans into a protective antibody. J. Immunol. 154: 1810– 1816.

109. Yuan, R. R.,, A. Casadevall,, J. Oh,, and M. D. Scharff. 1997. T cells cooperate with passive antibody to modify Cryptococcus neoformans infection in mice. Proc. Natl. Acad. Sci. USA 94: 2483– 2488.

110. Zitrin, C. M.,, and O. Wasz-Höckert. 1957. Preliminary experiments on passive transfer of protective humoral antibodies in tuberculosis. Am. Rev. Tuberc. Pulm. Dis. 76: 256– 262.

Tables

Role of Antibody-Mediated Immunity in Host Defense against Mycobacterium tuberculosis

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Table 1

Effect of MAbs on various aspects of mycobacterial infection

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10.1128/9781555817657/tab32-1.gif

Table 1

Effect of MAbs on various aspects of mycobacterial infection