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Titolo:
NONOPSONIC BINDING OF MYCOBACTERIUM-TUBERCULOSIS TO COMPLEMENT RECEPTOR-TYPE-3 IS MEDIATED BY CAPSULAR POLYSACCHARIDES AND IS STRAIN-DEPENDENT
Autore:
CYWES C; HOPPE HC; DAFFE M; EHLERS MRW;
Indirizzi:
UNIV CAPE TOWN,SCH MED,DEPT MED BIOCHEM ZA-7925 CAPE TOWN SOUTH AFRICA UNIV CAPE TOWN,SCH MED,DEPT MED BIOCHEM ZA-7925 CAPE TOWN SOUTH AFRICA CNRS,INST PHARMACOL & BIOL STRUCT F-31062 TOULOUSE FRANCE UNIV TOULOUSE 3 F-31062 TOULOUSE FRANCE
Titolo Testata:
Infection and immunity
fascicolo: 10, volume: 65, anno: 1997,
pagine: 4258 - 4266
SICI:
0019-9567(1997)65:10<4258:NBOMTC>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED MACROPHAGES; ALVEOLAR MACROPHAGES; TUBERCLE-BACILLI; PHAGOCYTOSIS; IDENTIFICATION; VIRULENT; MANNOSE; LECTIN; CELLS; ARABINOMANNANS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
C. Cywes et al., "NONOPSONIC BINDING OF MYCOBACTERIUM-TUBERCULOSIS TO COMPLEMENT RECEPTOR-TYPE-3 IS MEDIATED BY CAPSULAR POLYSACCHARIDES AND IS STRAIN-DEPENDENT", Infection and immunity, 65(10), 1997, pp. 4258-4266

Abstract

The choice of host cell receptor and the mechanism of binding (opsonic versus nonopsonic) may influence the intracellular fate of Mycobacterium tuberculosis. We have identified two substrains of M. tuberculosis H37Rv, designated H37Rv-CC and -HH, that differed in their modes of binding to complement receptor type 3 (CR3) expressed in transfected Chinese hamster ovary (CHO-Mac-l) cells: H37Rv-CC bound nonopsonically,whereas H37Rv-HH bound only after opsonization in fresh serum. H37Rv-CC also bound nonopsonically to untransfected CHO cells, whereas H37Rv-HH binding was enhanced by serum and was mediated by the 1D1 antigen,a bacterial adhesin previously identified as a polar phosphatidylinositol mannoside. H37Rv CC and -HH had identical IS6110 DNA fingerprint patterns. Of five M. tuberculosis clinical isolates examined, four displayed the same binding phenotype as H37Rv-CC, as did the Erdman strain, whereas one isolate, as well as Mycobacterium smegmatis, behaved like H37Rv-HH. Nonopsonic binding of H37Rv-CC to CHO cell-expressed CR3 was apparently to the beta-glucan lectin site, as it was cation independent and inhibited by laminarin (seaweed beta-glucan) and N-acetylglucosamine; laminarin also inhibited the binding of H37Rv-CC to monocyte-derived macrophages. Further, binding of H37Rv-CC to CHO-Mac-1 cells was inhibited by prior agitation of bacteria with glass beads (which strips outer capsular polysaccharides) and by preincubation with amyloglucosidase, as well as by the presence of capsular D-glucan and D-mannan from M. tuberculosis Erdman, but not by Erdman D-arabino-D-mannan, yeast mannan, or capsular components from H37Rv-HH. Analysis of capsular carbohydrates revealed that H37Rv-CC expressed 5-fold more glucose and 2.5-fold more arabinose and mannose than H37Rv-HH. Flow cytometricdetection of surface epitopes indicated that H37Rv-CC displayed twofold less surface-exposed phosphatidylinositol mannoside and bound complement C3 less efficiently than H37Rv-HH; these differences were eliminated after treatment of H37Rv-CC with glass beads. Thus, outer capsular polysaccharides mediate the binding of H37Rv-CC to CR3, likely to the beta-glucan site. Moreover, there are strain-dependent differences in the thickness or composition of capsular polysaccharides that determine the mode of binding of M. tuberculosis to mammalian cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 23:05:29