Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence
Mem. Inst. Oswaldo Cruz
;
107(supl.1): 174-182, Dec. 2012. ilus, graf
Article
Dans Anglais
| LILACS
| ID: lil-659756
ABSTRACT
When grown in the presence of exogenous collagen I, Mycobacterium bovis BCG was shown to form clumps. Scanning electron microscopy examination of these clumps revealed the presence of collagen fibres cross-linking the bacilli. Since collagen is a major constituent of the eukaryotic extracellular matrices, we assayed BCG cytoadherence in the presence of exogenous collagen I. Collagen increased the interaction of the bacilli with A549 type II pneumocytes or U937 macrophages, suggesting that BCG is able to recruit collagen to facilitate its attachment to host cells. Using an affinity chromatography approach, we have isolated a BCG collagen-binding protein corresponding to the previously described mycobacterial laminin-binding histone-like protein (LBP/Hlp), a highly conserved protein associated with the mycobacterial cell wall. Moreover, Mycobacterium leprae LBP/Hlp, a well-characterized adhesin, was also able to bind collagen I. Finally, using recombinant fragments of M. leprae LBP/Hlp, we mapped the collagen-binding activity within the C-terminal domain of the adhesin. Since this protein was already shown to be involved in the recognition of laminin and heparan sulphate-containing proteoglycans, the present observations reinforce the adhesive activities of LBP/Hlp, which can be therefore considered as a multifaceted mycobacterial adhesin, playing an important role in both leprosy and tuberculosis pathogenesis.
Texte intégral:
Disponible
Indice:
LILAS (Amériques)
Sujet Principal:
Adhérence bactérienne
/
Collagène de type I
/
Mycobacterium bovis
/
Mycobacterium leprae
Limites du sujet:
Animaux
/
Humains
langue:
Anglais
Texte intégral:
Mem. Inst. Oswaldo Cruz
Thème du journal:
Médecine tropicale
/
Parasitologie
Année:
2012
Type:
Article
Pays d'affiliation:
Brésil
Institution/Pays d'affiliation:
Fiocruz/BR
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