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Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5089, Institut de Pharmacologie et de Biologie Structurale, Toulouse, France
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Abstract |
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Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The contact between neutrophils and micro-organisms occurs frequently in tissues after a lesion or in organs directly exposed to the environment, such as the respiratory tract or the digestive mucosa. Under these conditions, neutrophils are in contact with infectious agents that are not covered by serum opsonins, such as Abs and complement factors. Paradoxically, receptors able to recognize and internalize bacteria under nonopsonic conditions have been little studied in neutrophils, whereas opsonic receptors have been the aim of extensive studies. In macrophages, several pattern recognition receptors that directly recognize molecular determinants present at the surface of microbes have been described, but few of them are expressed in neutrophils (1, 2, 3, 4, 5, 6, 7).
The complement receptor 3 (CR3)3 has been described to function as a nonopsonic receptor in macrophages (3). It is also expressed in neutrophils (8). CR3 is a pattern recognition receptor initially identified as a specific receptor for the complement fragment C3bi. It is also a receptor for extracellular matrix proteins such as fibronectin and therefore belongs to the ß2 integrin family, and finally, it is a lectin recognizing a large variety of sugars (3, 8, 9). CR3 is a heterodimer consisting of CD18, the protein common to proteins of the ß2 integrin family and CD11b, which contains the lectin site, the C3bi binding site, and the recognition domain of matrix proteins. This receptor has been involved in the selective internalization of pathogenic mycobacteria such as Mycobacterium kansasii in macrophages and in Chinese hamster ovary (CHO) cells stably expressing human CR3 (10, 11). M. kansasii remains a significant cause of human disease and is one of the most frequent nontuberculous mycobacterial pathogens isolated from clinical specimens (12). We have previously been involved in the study of bactericidal responses elicited by mycobacteria when they infect human neutrophils under nonopsonic conditions. We have reported that their phagocytosis elicits the production of O2- and the release of specific granule proteins, but the fusion of lysosomes with phagosomes was not triggered (13). Here we have tried to identify receptors involved in the phagocytosis of M. kansasii by human neutrophils. We report that CR3 plays a critical role in association with GPI-anchored proteins and depends on cholesterol.
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Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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Ficoll and dextran T500 were obtained from Amersham Pharmacia
Biotech (Courtaboeuf, France). FITC was purchased from Molecular Probes
(Eugene, OR). PBS, MEM, and HEPES were obtained from Life Technologies
(Cergy-Pontoise, France). Nystatin, ß-cyclodextrin, filipin,
N-acetyl-D-glucosamine (NADG),
zymosan A (Z), rabbit anti-mouse IgG-TRITC, goat anti-rabbit
IgG-FITC, and goat anti-rabbit-TRITC were obtained from Sigma
(Saint Quentin Fallavier, France). Mouse mAbs anti-CD55 (clone
JS11, IgG1; Sixth International Workshop on Human Leukocyte
Differentiation Ags) were provided by A. Bensussan (Institut National
de la Santé et de la Recherche Médicale, Unité 448,
Creteil, France). Mouse monoclonal anti-CD16b (clone 3G8, IgG1),
3G8-FITC, and rabbit polyclonal IgG anti-Hck were obtained from
Santa Cruz Biotechnology (Le Perray en Yvelines, France).
F(ab')2 of 3G8 were provided by C. Sautès
(Institut National de la Santé et de la Recherche Médicale,
Unité 225, Paris, France). Mouse monoclonal anti-CD14 (clone
MY4, IgG2a K) and anti-CD66b (clone 80H3, IgG1 
) were purchased
from Beckman Coulter (Gagny, France). Mouse anti-human CR3 (clone
2LPM19C, IgG1 K) and human anti-HLA class I (clone W6/32, IgG2a K)
were obtained from Dako (Trappes, France). Mouse monoclonal
anti-CD16b (clone 7.5.4, IgG1) was provided by J. L. Teillaud
(Institut National de la Santé et de la Recherche Médicale,
Unité 225, Paris, France) (14). The rabbit Ab
anti-mycobacterium, Camelia, has been previously described
(10). Phosphatidylinositol phospholipase C (PIPLC) was
purchased from Roche (Meylan, France).
Human neutrophils
Neutrophils were isolated from the blood of healthy donors by the dextran-Ficoll method as previously described (13), resuspended in MEM and 20 mM HEPES, pH 7.4, and maintained for 20 min at 37°C before stimulation.
Mycobacteria
M. kansasii (no. 124478, American Type Culture Collection, Manassas, VA) were prepared as previously described (13). Briefly, they were grown at 37°C as surface pellicles in 250-ml flasks containing 100 ml of Sauton broth medium. The medium was discarded, and the pellicles were disrupted by gentle shaking with glass beads (4 mm in diameter) for 30 min and resuspended in PBS, pH 7.4. To remove clumps, the bacterial suspensions were sedimented for 10 min, and supernatants were collected and centrifuged at 200 x g for 10 min. Mycobacteria in the supernatants were collected and counted under a microscope (Leica, Rueil-Malmaison, France) in a Thoma chamber, supplemented with 10% glycerol and stored at -80°C until use.
FITC staining of bacteria
Mycobacteria were labeled with FITC as previously described (13). Briefly, 1 x 109 bacteria were added to 10 ml of 0.005% FITC in 0.2 M Na2CO3/NaHCO3 and 150 mM NaCl buffer, pH 9.2, for 15 min. The bacteria were washed twice and resuspended in 1.5 ml of PBS, pH 7.4.
Opsonisation of FITC-stained bacteria or Z
Opsonisation was performed as previously described (13). Briefly, FITC-stained bacteria or Z (wall particles from Saccharomyces cerevisiae, which consist of glucan and mannan) were incubated with pooled human sera for 25 min at 37°C, washed twice, and suspended in PBS, pH 7.4.
Phagocytosis measurement and indirect immunofluorescence
Measurement of phagocytosis was performed as previously described (10, 13). Neutrophils adhering on glass coverslips (15) were exposed to FITC-stained mycobacteria (50 bacteria/cells) for 45 min, washed three times, and fixed with 3.7% paraformaldehyde in PBS containing 15 mM sucrose, pH 7.4, for 30 min at room temperature. After neutralizing with 50 mM NH4Cl, slides were washed in PBS, and labeling of extracellular mycobacteria was performed using the rabbit polyclonal Ab, Camelia, directed against mycobacteria (1/50) revealed by tetramethylrhodamine isothiocyanate-conjugated second Abs (1/100). Fluorescent green and red bacteria were extracellular. Cells containing fluorescent green mycobacteria were counted by fluorescence microscopy (Leica).
Phagosomes of neutrophils that had ingested Z or opsonised zymosan (OZ; 20 particles/cells) were visualized using anti-Hck Abs. This protein tyrosine kinase has been previously described to accumulate at the membrane of phagosomes containing these particles (4, 16), facilitating the detection of Z- or OZ-positive phagocytes. Cells stimulated with Z or OZ were washed three times, fixed, and permeabilized in methanol at -20°C for 6 min. After two washes in PBS-0.1% Tween 20, cells were incubated with affinity-purified anti-Hck Abs (1/200) and then with FITC-conjugated secondary Abs to stain the membrane of phagosomes. Cells with Hck-stained phagosomes were counted by fluorescence microscopy. For each condition at least 100 cells were counted.
Drug treatment
Adherent neutrophils (7 x 105 cells/ml in 20 mM MEM-HEPES, pH 7.4) were exposed to NADG (0.1 and 0.15 M), filipin (2 µg/ml), cyclodextrin (10 mM), or nystatin (25 µg/ml) for 15 min at 37°C. Cells were then incubated with FITC-stained bacteria (50 bacteria/cells) or with Z or OZ (20 particles/cells) as described above.
PIPLC treatment
Neutrophils in suspension were incubated with PIPLC (0.1 IU/ml) for 30 min at 37°C. Cell adhesion on glass coverslips was then performed in the presence of PIPLC. To avoid translocation of the intracellular pools of GPI-linked receptors to the plasma membrane (17, 18, 19), cells were maintained at 4°C during the adhesion procedure and washed with cold MEM-HEPES (20 mM), pH 7.4. Cells were then exposed to mycobacteria (50 bacteria/cells) or OZ (20 particles/cells) for 20 min at 4°C and washed with cold MEM-HEPES to remove nonadherent particles. Internalization of particles was induced by placing the cells at 37°C for 45 min.
Ab treatment
Adherent neutrophils were incubated for 15 min at 37°C with Abs directed against GPI-anchored proteins of neutrophils (3G8, 2.5 µg/ml; 3G8 F(ab')2, 2.5 µg/ml; 7.5.4, 2.5 µg/ml; MY4, 7.5 µg/ml; 80H3, 5 µg/ml; Js11, dilution 1/2), against a plasma membrane protein (anti-HLA class I, clone W6/32, 2.5 µg/ml) or against CR3 (2LPM19c, 2 µg/ml) and exposed to FITC-stained bacteria for 30 min at 37°C or to opsonised or nonopsonized Z for 15 min at 37°C. Cells were washed three times in PBS, pH 7.4, and fixed in paraformaldehyde.
FACS analysis
Cells in suspension were incubated with mouse anti-HLA (2.5 µg/ml) or FITC-conjugated anti-CD16b (3G8, 1/100) Abs at 4°C for 30 min and were washed twice in ice-cold PBS, pH 7.4, and fixed in paraformaldehyde. Anti-HLA Abs fixed on neutrophils were revealed by anti-mouse FITC-conjugated Abs (1/100). Fluorescence was measured by FACS analysis (FACScan, Becton Dickinson, Le Pont de Claix, France).
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Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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To test the involvement of CR3 in phagocytosis, neutrophils were
incubated with M. kansasii, Z, or OZ in the presence
or the absence of the mouse mAbs 2LPM. Z and OZ are known to be
internalized by CR3 (20). 2LPM Abs recognize an epitope
located in the I domain of CD11b (11). We found that in
the presence of Abs, the phagocytosis of Z and OZ was inhibited by 40
and 50%, respectively, whereas the phagocytosis of M.
kansasii was inhibited by 90% (Fig. 1
).
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Cholesterol and GPI-linked proteins are involved in the phagocytosis of M. kansasii
To test the involvement of GPI-linked proteins in phagocytosis of
M. kansasii, we first treated cells with
cholesterol-scavenging (ß-cyclodextrin) or -binding (filipin or
nystatin) molecules, because it has been shown to affect the function
of raft-associated proteins (31, 32, 33, 34). Neutrophils were
exposed to 10 mM cyclodextrin for 15 min and mycobacteria, Z, or OZ
were then added to the cells. As shown in Fig. 2A, phagocytosis of M.
kansasii was strongly inhibited. Similar results were obtained
with filipin and nystatin, indicating that despite their distinct modes
of action on membrane cholesterol, the three molecules exert efficient
inhibitory action on phagocytosis of M. kansasii (Fig. 2A). In addition, none of these molecules had a cytotoxic
effect, because phagocytosis of Z was as efficient as that in control
cells. Interestingly, when M. kansasii were serum opsonized,
the inhibitory effect of cholesterol-depleting molecules was not
observed (Fig. 2B), further supporting the lack of
cytotoxicity discussed above and indicating that internalization of
mycobacteria through opsonic receptors is not affected by cholesterol
binding or scavenging molecules.
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RIII, 200,000
sites/cell), as shown by FACS analysis (Fig. 3A). However, it has been
previously described that not all the GPI-anchored proteins can be
removed by PIPLC (36). After treatment of neutrophils with
PIPLC, phagocytosis of M. kansasii, but not of Z, was
inhibited (Fig. 3B). These results indicate that PIPLC has a
specific inhibitory effect on phagocytosis of mycobacteria, most likely
the result of removal of GPI-anchored proteins from the cell surface.
It is interesting to note that internalization of OZ was not affected
by removing CD16b from the cell surface, indicating that the other IgG
receptors expressed in neutrophils in concert with complement receptors
(37) are sufficient to maintain a constant rate of opsonic
phagocytosis.
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. All the Abs were found to inhibit
phagocytosis of M. kansasii, but not phagocytosis of OZ
(Fig. 4A) or Z (data not shown).
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B) but did not interfere with phagocytosis of OZ, M.
kansasii (Fig. 4A), or Z (not shown). Moreover,
F(ab')2 of 3G8 were as efficient as the
corresponding Ig to inhibit phagocytosis of M. kansasii
(Fig. 4A). In conclusion, phagocytosis of M. kansassii is inhibited by 1) molecules that sequester cholesterol; 2) PIPLC, which removes GPI-anchored proteins from the cell surface; and 3) Abs directed against CR3 or GPI receptors. These data suggest that GPI receptors associate with CR3 in cholesterol-rich domains, triggering the entry of these bacteria in human neutrophils.
3-NADG inhibits phagocytosis of mycobacteria
To determine whether association of GPI-linked proteins to CR3 is
critical for phagocytosis of M. kansasii, neutrophils were
incubated with NADG, a saccharide previously shown to disrupt the
interaction between CR3 and GPI-linked receptors such as CD16b and CD59
(38, 39). This saccharide binds to the lectin site of CR3
shown to be involved in the recognition of GPI-linked proteins of Z,
but not of mycobacteria (10, 40). As expected, in
the presence of NADG, phagocytosis of Z, but not that of OZ, was
inhibited. In addition, internalization of M. kansasii was
strongly inhibited (Fig. 5).
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The nonopsonic receptors involved in phagocytosis of M. kansasii in neutrophils are not known. We found that Abs against CR3 inhibit the entry of M. kansasii, implying that CR3 is one such receptor. CR3 is known to associate with several GPI-anchored receptors (8, 21, 22, 23, 24), suggesting that CR3 may be localized in rafts. However, we also found that CR3 is involved to some extent in the phagocytosis of Z and OZ, whose phagocytosis was not affected by cholesterol-depleting or -sequestering agents. Therefore, there must also be a population of CR3 outside of rafts.
Binding of GPI-linked proteins by CR3 could result in its translocation to rafts, and if we assume that these events would render CR3 capable of binding M. kansasii, this would explain why we could equally well inhibit M. kansasii phagocytosis by Abs against a variety of GPI-linked proteins. Therefore, we think that CR3, rather than any specific GPI-linked proteins, functions as the M. kansasii receptor, but that CR3 requires cholesterol and association with GPI proteins (as discussed below) to internalize M. kansasii. Although several GPI-linked proteins have been shown to interact with micro-oganisms (35, 42, 43), our observation that all the Abs directed against GPI proteins display an inhibitory effect on the phagocytosis of M. kansasii eliminates the possibility that a GPI protein could be its receptor. More likely, binding of Abs to GPI proteins might impair (steric hindrance) their association with CR3, which, consequently, remains unable to internalize M. kansasii. GPI-anchored proteins are devoid of transmembrane and intracellular domains. They cooperate with CR3 to mediate intracellular signaling, as demonstrated by several groups (22, 23, 24). Conversely, association of GPI-linked proteins with CR3 has been shown to enhance the activity of CR3 (23, 29, 30), probably because this association produces conformational changes in CR3. Indeed, a high affinity state of CR3 has been proposed to explain its enhanced phagocytic or adhesion capacity when it is phophorylated or associated with proteins or sugars (3, 8, 44). The interaction between CD16b or CD87 and CR3 is mediated by the glycosylated moieties of the GPI-anchored proteins and the lectin domain of CD11b. Interactions between CR3 and the other GPI proteins are probably of the same nature, because all GPI proteins expressed in neutrophils are heavily glycosylated (45). This interaction can be inhibited by sugars such as NADG (28, 38, 39). Here we show that NADG was able to inhibit phagocytosis of M. kansasii, further suggesting that association of GPI proteins with CR3 is necessary to mediate phagocytosis. If the human CR3 is expressed in nonphagocytic CHO cells, NADG has no inhibitory effect, and CR3 mediates phagocytosis of M. kansasii very slowly compared with neutrophils (10), suggesting that CR3 may not be associated with GPI-anchored proteins in CHO cells.
Therefore, to internalize M. kansasii in human neutrophils, we propose that CR3 needs to associate with GPI receptors in cholesterol-rich domains. In contrast, when CR3 is not associated with a GPI protein, it remains outside of cholesterol-rich domains where it can mediate phagocytosis of Z and OZ, but not that of M. kansasii.
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Acknowledgments |
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Footnotes |
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2 Address correspondence and reprint requests to Dr. Isabelle Maridonneau-Parini, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5089, Institut de Pharmacologie et de Biologie Structurale, Toulouse, France.
3 Abbreviations used in this paper: CR3, complement receptor 3; NADG, N-acetyl-D-glucosamine; Z, zymosan A; PIPLC, phosphatidylinositol phospholipase C; OZ, opsonised zymosan; CHO, Chinese hamster ovary.
Received for publication June 13, 2000. Accepted for publication August 4, 2000.
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C. Cougoule, P. Constant, G. Etienne, M. Daffe, and I. Maridonneau-Parini Lack of Fusion of Azurophil Granules with Phagosomes during Phagocytosis of Mycobacterium smegmatis by Human Neutrophils Is Not Actively Controlled by the Bacterium Infect. Immun., March 1, 2002; 70(3): 1591 - 1598. [Abstract] [Full Text] [PDF]
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A. Naroeni and F. Porte Role of Cholesterol and the Ganglioside GM1 in Entry and Short-Term Survival of Brucella suis in Murine Macrophages Infect. Immun., March 1, 2002; 70(3): 1640 - 1644. [Abstract] [Full Text] [PDF]
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 C. Astarie-Dequeker, S. Carreno, C. Cougoule, and I. Maridonneau-Parini The protein tyrosine kinase Hck is located on lysosomal vesicles that are physically and functionally distinct from CD63-positive lysosomes in human macrophages J. Cell Sci., January 1, 2002; 115(1): 81 - 89. [Abstract] [Full Text] [PDF]
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J. G. Marshall, J. W. Booth, V. Stambolic, T. Mak, T. Balla, A. D. Schreiber, T. Meyer, and S. Grinstein Restricted Accumulation of Phosphatidylinositol 3-Kinase Products in a Plasmalemmal Subdomain during Fc{gamma} Receptor-Mediated Phagocytosis J. Cell Biol., June 25, 2001; 153(7): 1369 - 1380. [Abstract] [Full Text] [PDF]
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P. Peyron, I. Maridonneau-Parini, and T. Stegmann Fusion of Human Neutrophil Phagosomes with Lysosomes in Vitro. INVOLVEMENT OF TYROSINE KINASES OF THE Src FAMILY AND INHIBITION BY MYCOBACTERIA J. Biol. Chem., September 14, 2001; 276(38): 35512 - 35517. [Abstract] [Full Text] [PDF]
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