Abstract
Mycobacteria reside intracellularly in a vacuole that allows it to circumvent the antimicrobial environment of the host macrophage. Although the mycobacterial phagosome exhibits selective fusion with vesicles of the endosomal system, identification of host and bacterial factors associated with phagosome biogenesis is limited. To identify these potential factors, mAbs were generated to a membrane preparation of mycobacterial phagosomes isolated from M. tuberculosis-infected macrophages. A mAb recognizing a 32-35 kDa macrophage protein associated with the phagosomal membrane of Mycobacterium was identified. N-terminal sequence analysis identified this protein as Mac-2 or galectin-3, a galactoside-binding protein of macrophages. Galectin-3 (gal-3) was shown to accumulate in Mycobacterium-containing phagosomes during the course of infection. This accumulation was specific for phagosomes containing live mycobacteria and occurred primarily at the cytosolic face of the phagosome membrane. In addition, binding of gal-3 to mycobacterial phosphatidylinositol mannosides (PIMs) demonstrated a novel interaction between host carbohydrate-binding proteins and released mycobacterial glycolipids. Infection of macrophages from gal-3-deficient mice indicated that the protein did not play a role in infection in vitro. In contrast, infection of gal-3-deficient mice revealed a reduced capacity to clear late but not early infection.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 167-176 |
| Number of pages | 10 |
| Journal | Cellular Microbiology |
| Volume | 4 |
| Issue number | 3 |
| DOIs | |
| State | Published - 2002 |
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ASJC Scopus subject areas
- Clinical Biochemistry
- Microbiology
Cite this
Association of a macrophage galactoside-binding protein with Mycobacterium-containing phagosomes. / Beatty, Wandy L.; Rhoades, Elizabeth R.; Hsu, Daniel K.; Liu, Fu-Tong; Russell, David G.
In: Cellular Microbiology, Vol. 4, No. 3, 2002, p. 167-176.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Association of a macrophage galactoside-binding protein with Mycobacterium-containing phagosomes
AU - Beatty, Wandy L.
AU - Rhoades, Elizabeth R.
AU - Hsu, Daniel K.
AU - Liu, Fu-Tong
AU - Russell, David G.
PY - 2002
Y1 - 2002
N2 - Mycobacteria reside intracellularly in a vacuole that allows it to circumvent the antimicrobial environment of the host macrophage. Although the mycobacterial phagosome exhibits selective fusion with vesicles of the endosomal system, identification of host and bacterial factors associated with phagosome biogenesis is limited. To identify these potential factors, mAbs were generated to a membrane preparation of mycobacterial phagosomes isolated from M. tuberculosis-infected macrophages. A mAb recognizing a 32-35 kDa macrophage protein associated with the phagosomal membrane of Mycobacterium was identified. N-terminal sequence analysis identified this protein as Mac-2 or galectin-3, a galactoside-binding protein of macrophages. Galectin-3 (gal-3) was shown to accumulate in Mycobacterium-containing phagosomes during the course of infection. This accumulation was specific for phagosomes containing live mycobacteria and occurred primarily at the cytosolic face of the phagosome membrane. In addition, binding of gal-3 to mycobacterial phosphatidylinositol mannosides (PIMs) demonstrated a novel interaction between host carbohydrate-binding proteins and released mycobacterial glycolipids. Infection of macrophages from gal-3-deficient mice indicated that the protein did not play a role in infection in vitro. In contrast, infection of gal-3-deficient mice revealed a reduced capacity to clear late but not early infection.
AB - Mycobacteria reside intracellularly in a vacuole that allows it to circumvent the antimicrobial environment of the host macrophage. Although the mycobacterial phagosome exhibits selective fusion with vesicles of the endosomal system, identification of host and bacterial factors associated with phagosome biogenesis is limited. To identify these potential factors, mAbs were generated to a membrane preparation of mycobacterial phagosomes isolated from M. tuberculosis-infected macrophages. A mAb recognizing a 32-35 kDa macrophage protein associated with the phagosomal membrane of Mycobacterium was identified. N-terminal sequence analysis identified this protein as Mac-2 or galectin-3, a galactoside-binding protein of macrophages. Galectin-3 (gal-3) was shown to accumulate in Mycobacterium-containing phagosomes during the course of infection. This accumulation was specific for phagosomes containing live mycobacteria and occurred primarily at the cytosolic face of the phagosome membrane. In addition, binding of gal-3 to mycobacterial phosphatidylinositol mannosides (PIMs) demonstrated a novel interaction between host carbohydrate-binding proteins and released mycobacterial glycolipids. Infection of macrophages from gal-3-deficient mice indicated that the protein did not play a role in infection in vitro. In contrast, infection of gal-3-deficient mice revealed a reduced capacity to clear late but not early infection.
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UR - http://www.scopus.com/inward/citedby.url?scp=0036207005&partnerID=8YFLogxK
U2 - 10.1046/j.1462-5822.2002.00183.x
DO - 10.1046/j.1462-5822.2002.00183.x
M3 - Article
C2 - 11906453
AN - SCOPUS:0036207005
VL - 4
SP - 167
EP - 176
JO - Cellular Microbiology
JF - Cellular Microbiology
SN - 1462-5814
IS - 3
ER -