| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
National Hansen’s Disease Programs, Laboratory Research Branch, Louisiana State University School of Veterinary Medicine, Baton Rouge, LA 70803
The lepromatous leprosy granuloma is a dynamic entity requiring a steady influx of macrophages (M
) for its maintenance. We have developed an in vitro model to study the fate of Mycobacterium leprae in a LL lesion, with and without immunotherapeutic intervention. Target cells, consisting of granuloma M harvested from the footpads of M. leprae-infected athymic nu/nu mice, were cocultured with normal or IFN-
-activated (ACT) effector M. The bacilli were recovered and assessed for viability by radiorespirometry. M. leprae recovered from target M possessed high metabolic activity, indicating a viable state in this uncultivable organism. M. leprae recovered from target M incubated with normal effector M exhibited significantly higher metabolism. In contrast, bacilli recovered from target M cocultured with ACT effector M displayed a markedly decreased metabolic activity. Inhibition by ACT M required an E:T ratio of at least 5:1, a coculture incubation period of 3–5 days, and the production of reactive nitrogen intermediates, but not reactive oxygen intermediates. Neither IFN- nor TNF-
were required during the cocultivation period. However, cell-to-cell contact between the target and effector M was necessary for augmentation of M. leprae metabolism by normal effector M as well as for inhibition of M. leprae by ACT effector M. Conventional fluorescence microscopy and confocal fluorescence microscopy revealed that the bacilli from the target M were acquired by the effector M. Thus, the state of M infiltrating the granuloma may markedly affect the viability of M. leprae residing in M in the lepromatous lesion.
This article has been cited by other articles:
|
|
 |
|
  T. Mukai, Y. Maeda, T. Tamura, M. Matsuoka, Y. Tsukamoto, and M. Makino Induction of Cross-Priming of Naive CD8+ T Lymphocytes by Recombinant Bacillus Calmette-Guerin That Secretes Heat Shock Protein 70-Major Membrane Protein-II Fusion Protein J. Immunol., November 15, 2009; 183(10): 6561 - 6568. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. A. Hagge, B. M. Saunders, G. J. Ebenezer, N. A. Ray, V. T. Marks, W. J. Britton, J. L. Krahenbuhl, and L. B. Adams Lymphotoxin-{alpha} and TNF Have Essential but Independent Roles in the Evolution of the Granulomatous Response in Experimental Leprosy Am. J. Pathol., April 1, 2009; 174(4): 1379 - 1389. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. L. Williams, T. L. Pittman, M. Deshotel, S. Oby-Robinson, I. Smith, and R. Husson Molecular Basis of the Defective Heat Stress Response in Mycobacterium leprae J. Bacteriol., December 15, 2007; 189(24): 8818 - 8827. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Makino, Y. Maeda, and K. Inagaki Immunostimulatory Activity of Recombinant Mycobacterium bovis BCG That Secretes Major Membrane Protein II of Mycobacterium leprae. Infect. Immun., November 1, 2006; 74(11): 6264 - 6271. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. M. Scollard, L. B. Adams, T. P. Gillis, J. L. Krahenbuhl, R. W. Truman, and D. L. Williams The Continuing Challenges of Leprosy Clin. Microbiol. Rev., April 1, 2006; 19(2): 338 - 381. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
