Mycobacteria use their surface-exposed glycolipids to infect human macrophages through a receptor-dependent process

Two subfamilies of the polar glycopeptidolipids (GPLs) located on the surface of Mycobacterium smegmatis, along with unknown phospholipids, were recently shown to participate in the nonopsonic phagocytosis of mycobacteria by human macrophages (Villeneuve, C., G. Etienne, V. Abadie, H. Montrozier, C. Bordier, F. Laval, M. Daffe, I. Maridonneau-Parini, and C. Astarie-Dequeker. 2003. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of glycopeptidolipids. J. Biol. Chem. 278: 51291–51300). As demonstrated herein, a phospholipid mixture that derived from the methanol-insoluble fraction inhibited the phagocytosis of M. smegmatis. Inhibition was essentially attributable to phosphatidylinositol mannosides (PIMs), namely PIM2 and PIM6, because the purified phosphatidylethanolamine, phosphatidylglycerol, and phosphatidylinositol were inactive. This was further confirmed using purified PIM2 and PIM6 from M. bovis BCG that decreased by half the internalization of M. smegmatis. Both compounds also inhibited the uptake of M. tuberculosis and M. avium but had no effect on the internalization of zymosan used as a control particle of the phagocytic process. When coated on latex beads, PIM2 and polar GPL (GPL III) favored the particle entry through complement receptor 3. GPL III, but not PIM2, also directed particle entry through the mannose receptor.Therefore, surface-exposed mycobacterial PIM and polar GPL participate in the receptor-dependent internalization of mycobacteria in human macrophages. Two subfamilies of the polar glycopeptidolipids (GPLs) located on the surface of Mycobacterium smegmatis, along with unknown phospholipids, were recently shown to participate in the nonopsonic phagocytosis of mycobacteria by human macrophages (Villeneuve, C., G. Etienne, V. Abadie, H. Montrozier, C. Bordier, F. Laval, M. Daffe, I. Maridonneau-Parini, and C. Astarie-Dequeker. 2003. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of glycopeptidolipids. J. Biol. Chem. 278: 51291–51300). As demonstrated herein, a phospholipid mixture that derived from the methanol-insoluble fraction inhibited the phagocytosis of M. smegmatis. Inhibition was essentially attributable to phosphatidylinositol mannosides (PIMs), namely PIM2 and PIM6, because the purified phosphatidylethanolamine, phosphatidylglycerol, and phosphatidylinositol were inactive. This was further confirmed using purified PIM2 and PIM6 from M. bovis BCG that decreased by half the internalization of M. smegmatis. Both compounds also inhibited the uptake of M. tuberculosis and M. avium but had no effect on the internalization of zymosan used as a control particle of the phagocytic process. When coated on latex beads, PIM2 and polar GPL (GPL III) favored the particle entry through complement receptor 3. GPL III, but not PIM2, also directed particle entry through the mannose receptor. Therefore, surface-exposed mycobacterial PIM and polar GPL participate in the receptor-dependent internalization of mycobacteria in human macrophages. The outcome of mycobacterial infections is thought to be critically dependent on the nonopsonic invasion and colonization of macrophages during primary infection of inhaled bacteria. This is why the initial step of mycobacteria phagocytosis by macrophages received considerable attention, including efforts to delineate the molecular mechanisms that underlie this process. Nonopsonic internalization of mycobacteria in macrophages can be mediated by different kinds of receptors that specifically recognize ligands expressed at the surface of bacilli (1Ernst J.D. Macrophage receptors for Mycobacterium tuberculosis.Infect. Immun. 1998; 66: 1277-1281Crossref PubMed Google Scholar, 2Bermudez L.E. Sangari F.J. Cellular and molecular mechanisms of internalization of mycobacteria by host cells.Microbes Infect. 2001; 3: 37-42Crossref PubMed Scopus (25) Google Scholar). Glycophosphoinositol-anchored receptors such as CD14 (3Peterson P.K. Gekker G. Hu S. Sheng W.S. Anderson W.R. Ulevitch R.J. Tobias P.S. Gustafson K.V. Molitor T.W. Chao C.C.C. CD14 receptor-mediated uptake of nonopsonized Mycobacterium tuberculosis by human microglia.Infect. Immun. 1995; 63: 1598-1602Crossref PubMed Google Scholar, 4Khanna K.V. Choi C.S. Gekker G. Peterson P.K. Molitor T.W.W. Differential infection of porcine alveolar macrophage subpopulations by nonopsonized Mycobacterium bovis involves CD14 receptors.J. Leukoc. Biol. 1996; 60: 214-220Crossref PubMed Scopus (21) Google Scholar), scavenger receptor (5Zimmerli S. Edwards S. Ernst J.D. Selective receptor blockade during phagocytosis does not alter the survival and growth of Mycobacterium tuberculosis in human macrophages.Am. J. Respir. Cell Mol. Biol. 1996; 15: 760-770Crossref PubMed Scopus (147) Google Scholar), and transferrin receptor (6Bermudez L.E. Parker A. Goodman J.R. Growth within macrophages increases the efficiency of Mycobacterium avium in invading other macrophages by a complement receptor-independent pathway.Infect. Immun. 1997; 65: 1916-1925Crossref PubMed Google Scholar, 7Roecklein J.A. Swartz R.P. Yeager Jr, H. Nonopsonic uptake of Mycobacterium avium complex by human monocytes and alveolar macrophages.J. Lab. Clin. Med. 1992; 119: 772-781PubMed Google Scholar) have been suggested as putative routes of entry for mycobacteria into macrophages. Additionally, complement receptor 3 (CR3) (8Schlesinger L.S. Macrophage phagocytosis of virulent but not attenuated strains of Mycobacterium tuberculosis is mediated by mannose receptors in addition to complement receptors.J. Immunol. 1993; 150: 2920-2930Crossref PubMed Google Scholar, 9Bermudez L.E. Young L.S. Enkel H. Interaction of Mycobacterium avium complex with human macrophages: roles of membrane receptors and serum proteins.Infect. Immun. 1991; 59: 1697-1702Crossref PubMed Google Scholar, 10Stokes R.W. Haidl I.D. Jefferies W.A. Speert D.P. Mycobacteria-macrophage interactions. Macrophage phenotype determines the nonopsonic binding of Mycobacterium tuberculosis to murine macrophages.J. Immunol. 1993; 151: 7067-7076PubMed Google Scholar) and mannose receptor (MR) (8Schlesinger L.S. Macrophage phagocytosis of virulent but not attenuated strains of Mycobacterium tuberculosis is mediated by mannose receptors in addition to complement receptors.J. Immunol. 1993; 150: 2920-2930Crossref PubMed Google Scholar, 11Astarie-Dequeker C. N'Diaye E.N. Cabec V. Le Rittig M.G. Prandi J. Maridonneau-Parini I.I. The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages.Infect. Immun. 1999; 67: 469-477Crossref PubMed Google Scholar) are both well-known receptors for the binding and internalization of mycobacteria in macrophages. Both receptors exhibited lectin-like properties. Indeed, MR is a monomeric transmembrane protein with an extracellular domain containing eight carbohydrate recognition domains with C-type lectin properties that recognize mannose, fucose, and N-acetylglucosamine residues present on the cell surface of pathogens, such as mycobacteria (12Pontow S.E. Kery V. Stahl P.D. Mannose receptor.Int. Rev. Cytol. 1992; 137B: 221-244PubMed Google Scholar, 13Largent B.L. Walton K.M. Hoppe C.A. Lee Y.C. Schnaar R.L.L. Carbohydrate-specific adhesion of alveolar macrophages to mannose-derivatized surfaces.J. Biol. Chem. 1984; 259: 1764-1769Abstract Full Text PDF PubMed Google Scholar, 14Stahl P. Schlesinger P.H. Sigardson E. Rodman J.S. Lee Y.C.C. Receptor-mediated pinocytosis of mannose glycoconjugates by macrophages: characterization and evidence for receptor recycling.Cell. 1980; 19: 207-215Abstract Full Text PDF PubMed Scopus (381) Google Scholar). CR3 is a heterodimeric type 1 transmembrane glycoprotein consisting of a CD18 β subunit noncovalently associated with the CD11b α chain. The extracellular portion of CD11b contained distinct functional binding domains. One of these, called the I domain, is essential for the recognition and internalization of C3bi opsonized particles (15Ross G.D. Vetvicka V. CR3 (CD11b, CD18): a phagocyte and NK cell membrane receptor with multiple ligand specificities and functions.Clin. Exp. Immunol. 1993; 92: 181-184Crossref PubMed Scopus (242) Google Scholar, 16Sengelov H. Complement receptors in neutrophils.Crit. Rev. Immunol. 1995; 15: 107-131Crossref PubMed Google Scholar). Another one, located on the carboxyl-terminal end of the extracellular portion of CD11b, is a nonopsonic binding site with lectin properties (17Thornton B.P. Vetvicka V. Pitman M. Goldman R.C. Ross G.D.D. Analysis of the sugar specificity and molecular of the lectin site of complement receptor type 3 Immunol. 1996; PubMed Google Scholar). This domain is in phagocytosis of particles containing such as zymosan G.D. J.A. complement receptor type (CR3) lectin-like properties to as as a receptor for zymosan and as as a receptor for Immunol. PubMed Google Scholar), but also with mannose, and (17Thornton B.P. Vetvicka V. Pitman M. Goldman R.C. Ross G.D.D. Analysis of the sugar specificity and molecular of the lectin site of complement receptor type 3 Immunol. 1996; PubMed Google Scholar). a nonopsonic binding domain distinct from the lectin been to and mycobacteria Cabec V. C. Maridonneau-Parini I. Nonopsonic phagocytosis of zymosan and Mycobacterium by CR3 involves distinct molecular and is is not with Immun. PubMed Scopus Google Scholar). recently demonstrated that mycobacteria at surface that a in internalization by human macrophages C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). a of phagocytosis that but not from the of Mycobacterium smegmatis by a the nonopsonic phagocytosis of mycobacteria by human macrophages the internalization of particles such as zymosan latex C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). of the that the compounds to the and phospholipid C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). When the family was and C-type were a novel of C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). have also that to inhibit the phagocytosis of mycobacteria is dependent on Identification of and putative as surface-exposed ligands of phagocytic receptors the at the molecular The present was to the mycobacteria surface-exposed that a in internalization by human macrophages and to the roles of and as ligands of phagocytic phosphatidylinositol and were from were from and were from the CD11b extracellular domain was used MR was a of P. Stahl was as Cabec V. C. Maridonneau-Parini I. Nonopsonic phagocytosis of zymosan and Mycobacterium by CR3 involves distinct molecular and is is not with Immun. PubMed Scopus Google Scholar). were from M. smegmatis and M. tuberculosis were as surface on at M. avium to as surface the was at in with is to that the of the surface-exposed is of growth surface G. C. H. C. The of the of glycopeptidolipids on the cell surface and cell and phagocytosis of Mycobacterium PubMed Scopus Google Scholar). cell were with for M. smegmatis, 3 for M. tuberculosis and M. as C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). smegmatis and M. were by the by for with of and in the of M. the was by at for the the were for at to of mycobacteria were and When mycobacteria were with as E.N. C. M. J. Maridonneau-Parini I.I. of with and of the are specifically inhibited during phagocytosis of mycobacteria by human Immunol. 1998; Google Scholar). that of internalization and of entry within macrophages derived from monocytes were to by M. smegmatis not a effect of and are present in both the of the cell and mycobacteria G. C. H. C. The of the of glycopeptidolipids on the cell surface and cell and phagocytosis of Mycobacterium PubMed Scopus Google Scholar, A. A. F. G. P. G. Identification of the surface-exposed on the cell of Mycobacterium tuberculosis and other mycobacterial 1996; PubMed Scopus Google Scholar). Therefore, the present was on from M. smegmatis to for further C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). were with and at with The were with and to were in a of and with for at methanol-insoluble were by at for were further using an were using a in in and in in and in of and was by were in were and in the of The of GPL been in C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). the were on a with and with a of of and in GPL I was with GPL was in polar with a mixture of the were further from using an of the were by on with for the compounds were by with in by the and were used to and mannosides type and and were purified on a as M. C. M. G. of the phosphatidylinositol mannosides from Mycobacterium bovis and to and Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar). of of was as F. C. M. molecular of by Chem. 2001; PubMed Scopus Google Scholar). were on a with a at and were in the using an at and an in of monocytes were as C. N'Diaye E.N. Cabec V. Le Rittig M.G. Prandi J. Maridonneau-Parini I.I. The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages.Infect. Immun. 1999; 67: 469-477Crossref PubMed Google Scholar) and for on on containing with serum in The was on the were with were coated as by and L.S. of the of from a virulent of Mycobacterium tuberculosis to human macrophages.J. Immunol. PubMed Google Scholar). of 1 were in were for 1 at with of in a of 1 The were in in for at in in and at the When were for at with the purified were in and for and with particles at the of the end of were with to of and latex was by as C. N'Diaye E.N. Cabec V. Le Rittig M.G. Prandi J. Maridonneau-Parini I.I. The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages.Infect. Immun. 1999; 67: 469-477Crossref PubMed Google Scholar). of were and at were by The of phagocytic at particle was as of phagocytic of are expressed as the of phagocytosis as of phagocytic in the control of phagocytic of phagocytic in the control are as of the of in The of the was by the present to the surface-exposed in the internalization of this from M. smegmatis was in by As in the methanol-insoluble by contained in PIM2 and PIM6 as the and of the effect of the methanol-insoluble fraction on phagocytosis was the to the of in the phagocytic of were for with the at from to and into with M. smegmatis for the and macrophages M. smegmatis and to in a in the uptake of M. smegmatis to This effect to the of the phospholipids, the effect of the addition of and on the phagocytosis of M. smegmatis. of for with not the internalization of M. smegmatis with purified from mycobacteria cell by not the phagocytosis of M. smegmatis with macrophages and suggested that the of the methanol-insoluble fraction was essentially attributable to This was further confirmed using from a M. smegmatis as methanol-insoluble were by into with of in and that the contained of not contained essentially PIM and Therefore, were on phagocytosis of M. smegmatis at the for the phospholipid As shown in the exhibited an effect of This of that were the compounds for the of the phospholipid mixture and were the essential in the phagocytic of PIM2 and PIM6 the mycobacterial to M. C. M. G. of the phosphatidylinositol mannosides from Mycobacterium bovis and to and Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar, M. G. of the phosphatidylinositol from Mycobacterium bovis and Mycobacterium tuberculosis and in receptor Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar, A. of phosphatidylinositol mannosides from Mycobacterium of a for and 1995; PubMed Scopus Google Scholar). As of PIM the of of M. smegmatis and were in PIM2 and PIM2 were in PIM6 and PIM6 in to PIM2 from PIM6 by the This to purified PIM2 and PIM6 subfamilies from M. bovis BCG by M. C. M. G. of the phosphatidylinositol mannosides from Mycobacterium bovis and to and Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar), are to of M. smegmatis M. G. of the phosphatidylinositol from Mycobacterium bovis and Mycobacterium tuberculosis and in receptor Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). As in both PIM2 and PIM6 subfamilies phagocytosis of M. smegmatis. from to of PIM6 of was at to PIM2 and PIM6 subfamilies not zymosan used as a control of phagocytic and 3 and a of the by the of PIM2 and PIM6 with the phagocytosis of the pathogenic mycobacteria M. avium and M. When at both compounds the internalization of of PIM were to an of phagocytosis of the pathogenic to was with of M. smegmatis demonstrated that subfamilies of PIM are in the nonopsonic phagocytic of that subfamilies of surface-exposed of M. smegmatis, GPL inhibit the phagocytosis of mycobacteria C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). have also demonstrated that the nonopsonic phagocytosis of both pathogenic and nonpathogenic mycobacteria by human is mediated at in by CR3 and MR C. N'Diaye E.N. Cabec V. Le Rittig M.G. Prandi J. Maridonneau-Parini I.I. The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages.Infect. Immun. 1999; 67: 469-477Crossref PubMed Google Scholar, C. P. G. M. Maridonneau-Parini I. of of with during phagocytosis of Mycobacterium smegmatis by human is not by the Immun. PubMed Scopus Google Scholar). Therefore, the of PIM and GPL to inhibit mycobacteria internalization by entry through receptors was and this latex were coated with purified PIM GPL using the by and L.S. of the of from a virulent of Mycobacterium tuberculosis to human macrophages.J. Immunol. PubMed Google Scholar). As PIM2 and PIM6 on the phagocytosis of PIM2, the of was from M. bovis BCG and used for the as of the PIM were also coated with GPL GPL I from M. smegmatis, of GPL that have been shown to different on C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). The of the coated to macrophages through MR CR3 was using a with directed receptors was for to both and nonopsonic internalization through CR3 Cabec V. C. Maridonneau-Parini I. Nonopsonic phagocytosis of zymosan and Mycobacterium by CR3 involves distinct molecular and is is not with Immun. PubMed Scopus Google Scholar, C. Hoppe Nonopsonic binding of Mycobacterium tuberculosis to human complement receptor type 3 expressed in Immun. 1996; PubMed Google Scholar, P. C. N'Diaye E.N. Maridonneau-Parini I. Nonopsonic phagocytosis of Mycobacterium by human on and is mediated by CR3 associated with Immunol. PubMed Scopus Google Scholar). and nonopsonized zymosan were used as CR3 binding particles Cabec V. C. Maridonneau-Parini I. Nonopsonic phagocytosis of zymosan and Mycobacterium by CR3 involves distinct molecular and is is not with Immun. PubMed Scopus Google Scholar) and as a not the internalization of and not As of with for at decreased the internalization of and nonopsonized zymosan but not the phagocytosis of also by the entry of both GPL and but not that of GPL I that entry of and GPL beads, but not that of coated with GPL involves The entry of through the MR was also using a C. N'Diaye E.N. Cabec V. Le Rittig M.G. Prandi J. Maridonneau-Parini I.I. The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages.Infect. Immun. 1999; 67: 469-477Crossref PubMed Google Scholar), a MR for to The mannose receptor to for to by 1997; Full Text Full Text PDF PubMed Scopus Google Scholar, P. The mannose receptor mediates of in by and Immunol. 1998; Google Scholar). and latex were used as and of C. N'Diaye E.N. Cabec V. Le Rittig M.G. Prandi J. Maridonneau-Parini I.I. The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages.Infect. Immun. 1999; 67: 469-477Crossref PubMed Google Scholar). this of GPL were as as coated with were As of with for at the internalization of not the phagocytosis of GPL both but decreased the phagocytosis of GPL that GPL through the that both PIM2 and GPL participate to the internalization of mycobacteria and are ligands of phagocytic receptors expressed at the surface of The cell also called a in the of pathogenic a mycobacteria and host of such as R.W. The of the cell of Mycobacterium tuberculosis as an the of the with macrophages.Infect. Immun. PubMed Scopus Google Scholar) and GPL C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar), have been in the with macrophages. of the mycobacterial cell have also been shown to host cell responses I.I. M. Interaction of mycobacterial with host 1998; 3: PubMed Google Scholar), but at the cell surface is a of that the of M. smegmatis contained that also participate in the nonopsonic phagocytosis of The by and C. from Biol. Chem. Full Text PDF PubMed Google Scholar) in the are on and are of to residues to the of the The as a mixture of compounds from by the of residues and The nonpathogenic M. smegmatis been to PIM PIM2 and PIM6 M. C. M. G. of the phosphatidylinositol mannosides from Mycobacterium bovis and to and Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar, M. G. of the phosphatidylinositol from Mycobacterium bovis and Mycobacterium tuberculosis and in receptor Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar), in with the of the PIM other of PIM have been in the M. C. M. G. of the phosphatidylinositol mannosides from Mycobacterium bovis and to and Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar), were because in Therefore, the of mycobacterial phagocytosis was essentially attributable to PIM2 and This was further confirmed using PIM2 and PIM6 from M. bovis of PIM decreased the internalization of M. smegmatis by of were to M. avium M. tuberculosis phagocytosis to the are on the surface of both pathogenic and nonpathogenic mycobacteria M. G. of the phosphatidylinositol from Mycobacterium bovis and Mycobacterium tuberculosis and in receptor Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar, A. M. The and other of virulent and 1996; PubMed Scopus Google Scholar). are in the surface of that are with the of of that can PIM and on phagocytic such as CR3 C. Hoppe Nonopsonic binding of Mycobacterium tuberculosis to human complement receptor type 3 expressed in Immun. 1996; PubMed Google Scholar). that at the surface of M. smegmatis, have a for the phagocytic receptors the of pathogenic A. A. F. G. and surface-exposed of 1996; PubMed Scopus Google Scholar), this why different PIM are to inhibit to a the phagocytosis of M. smegmatis and M. avium M. to be that the of a carbohydrate portion on phospholipid is for the because no effect but PIM2 the of the does not to be for the because PIM2 and PIM6 inhibited have that to a mycobacterial inhibited the nonopsonic binding of M. tuberculosis to murine macrophages R.W. Speert D.P. nonopsonic binding of Mycobacterium tuberculosis to murine macrophages.J. Immunol. 1995; Google Scholar, M.G. P. of mycobacterial on of Mycobacterium tuberculosis with macrophages.Infect. Immun. 2001; PubMed Scopus Google Scholar). This is in with the a be to in the of murine and human macrophages. with C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar), that surface-exposed PIM and GPL participate in the internalization of mycobacteria by macrophages as are ligands of phagocytic is that other of the mycobacterial such as and also be in the of bacilli with as by the of routes of entry of mycobacteria into host The molecular mechanisms by surface-exposed and participate in the phagocytosis of mycobacteria have been to participate in the receptor-mediated uptake of mycobacteria L.S. of the of from a virulent of Mycobacterium tuberculosis to human macrophages.J. Immunol. PubMed Google Scholar, C. M. Identification of phosphatidylinositol as a mycobacterial both and binding to Immun. 1997; 65: PubMed Google Scholar). have been shown to as an the binding of M. tuberculosis and M. smegmatis to with mannose binding protein C. M. Identification of phosphatidylinositol as a mycobacterial both and binding to Immun. 1997; 65: PubMed Google Scholar). that latex with PIM2 internalization through a through the lectin binding site of recognize the of as other have been to be ligands of the this and for the that at PIM2, not in with this receptor in cell As the of the was not for PIM of that PIM6 was not a of The of of GPL as a putative ligand of macrophages been that GPL the entry of particles through both CR3 and of the GPL is the that in GPL and is on the C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar). have not been to be by MR and and putative binding to receptors to be further that surface-exposed and coated on latex are ligands of CR3 of the entry of mycobacteria in macrophages. When used as as as C. G. V. H. C. F. M. Maridonneau-Parini I. Surface-exposed glycopeptidolipids of Mycobacterium smegmatis specifically inhibit the phagocytosis of mycobacteria by human macrophages. Identification of a novel family of Biol. Chem. 278: Full Text Full Text PDF PubMed Scopus Google Scholar) the internalization of mycobacteria but not that of the are to both MR and the that zymosan and mycobacteria distinct nonopsonic binding of the receptor Cabec V. C. Maridonneau-Parini I. Nonopsonic phagocytosis of zymosan and Mycobacterium by CR3 involves distinct molecular and is is not with Immun. PubMed Scopus Google Scholar) that the site in zymosan internalization does not recognize and that surface-exposed and with the nonopsonic receptors CR3 MR in the phagocytosis of of binding properties is the of this but to further the mycobacterial to macrophages bactericidal is a and as of mycobacteria also to for the control of macrophage The are to G. and C. for of the and to F. and H. for and This was in by

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