Mycobacterial laminin-binding histone-like protein mediates collagen-dependent cytoadherence

被引:7
作者
Dias, Andre Alves [1 ]
Raze, Dominique [2 ,4 ,5 ,6 ]
de Lima, Cristiana Soares [1 ]
Marques, Maria Angela de Melo [7 ]
Drobecq, Herve [3 ]
Debrie, Anne-Sophie [2 ,4 ,5 ,6 ]
Ribeiro-Guimaraes, Michelle Lopes [1 ]
Biet, Franck [8 ]
Vidal Pessolani, Maria Cristina [1 ]
机构
[1] Inst Oswaldo Cruz Fiocruz, Lab Microbiol Celular, Rio De Janeiro, RJ, Brazil
[2] INSERM, U1019, F-59045 Lille, France
[3] Inst Pasteur, Ctr Immunol & Biol Parasitaire, CNRS, UMR 8525, F-59019 Lille, France
[4] Inst Pasteur, Ctr Immunol & Biol Parasitaire, CNRS, UMR 8204, F-59019 Lille, France
[5] Inst Pasteur, CIIL, Lille, France
[6] Univ Lille N France, Lille, France
[7] Colorado State Univ, Dept Microbiol Immunol & Patol, Ft Collins, CO 80523 USA
[8] INRA, UR1282, Ctr Tours, F-37380 Nouzilly, France
来源
MEMORIAS DO INSTITUTO OSWALDO CRUZ | 2012年 / 107卷
关键词
mycobacteria; cytoadherence; collagen; histone-like protein; leprosy; tuberculosis; SURFACE PROTEIN; TUBERCULOSIS; ADHESIN; HEMAGGLUTININ; IDENTIFICATION; ATTACHMENT; RECEPTORS; BACTERIAL; CELLS; MOTIF;
D O I
10.1590/S0074-02762012000900025
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
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.
引用
收藏
页码:174 / +
页数:11
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