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Phagocytosis of Mycobacterium tuberculosis is mediated by human monocyte complement receptors and complement component C3.

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Schlesinger, L S, Bellinger-Kawahara, C G, Payne, N R, Horwitz, M A·1990·The Journal of Immunology

Abstract

We have examined the receptor-ligand interactions and the method of phagocytosis of virulent Mycobacterium tuberculosis by human monocytes. mAb against complement receptors (CR) inhibit adherence and phagocytosis of M. tuberculosis in fresh nonimmune serum. A mAb against the type 1 CR (CR1) inhibits adherence of M. tuberculosis by 40 +/- 5%, and three different mAb against the type 3 CR (CR3) each inhibit adherence by 39 +/- 5% to 47 +/- 4%. A mAb against CR1 used in combination with one of the three mAb against CR3 inhibits adherence by up to 64 +/- 7%. Most strikingly, two mAb used in combination against CR3 inhibit adherence by up to 81 +/- 2%. mAb against other monocyte surface Ag do not significantly influence adherence. In like fashion, mAb against CR but not other monocyte surface Ag inhibit adherence of preopsonized M. tuberculosis in the presence of heat-inactivated serum. By electron microscopy, monocytes ingest all M. tuberculosis that adhere in the presence of nonimmune serum; mAb against CR3 markedly inhibit ingestion. In contrast to CR, the FcR and the beta-glucan-inhibitable receptor for zymosan play little or no role in mediating M. tuberculosis adherence or ingestion. Adherence of M. tuberculosis is serum-dependent, requiring greater than or equal to 2.5% serum for optimal adherence. Heat inactivation of serum markedly reduces adherence of M. tuberculosis (75.5 +/- 7%) and preopsonization of bacteria enhances adherence by 2.9 +/- 0.4-fold. Adherence is also markedly reduced in C3- or factor B-depleted serum; repletion with C3 or factor B increases adherence by 2.1 +/- 0.4-fold and 1.86 +/- 0.05-fold, respectively. Fab anti-C3 IgG markedly inhibits monocyte adherence of preopsonized M. tuberculosis (71 +/- 1%). C component C3 is fixed to M. tuberculosis by the alternative C pathway as determined by a whole bacterial cell ELISA. Human monocytes ingest M. tuberculosis by conventional phagocytosis as viewed by electron microscopy. This study demonstrates that human monocyte CR1 and CR3 mediate phagocytosis of M. tuberculosis and C component C3 in serum is acting as the major bacterium-bound ligand.

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Metadata

Authors
Schlesinger, L. S., Bellinger-Kawahara, C. G., Payne, N. R., & Horwitz, M. A.
Venue
The Journal of Immunology
Published
1990-04-01
Volume
144
Issue
7
Pages
2771-2780
ISSN
  • 0022-1767 (ISSN-L)
  • 1550-6606
OpenAlex
W1557707473
Cited by
539
References
0
FWCI
13.36
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Phagocytosis of Mycobacterium tuberculosis is mediated by human monocyte complement receptors and complement component C3. https://app.cochat.ai/papers/10.4049/jimmunol.144.7.2771
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Schlesinger, L. S., Bellinger-Kawahara, C. G., Payne, N. R., & Horwitz, M. A. (1990). Phagocytosis of Mycobacterium tuberculosis is mediated by human monocyte complement receptors and complement component C3. The Journal of Immunology. https://doi.org/10.4049/jimmunol.144.7.2771

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