Roles of Soluble Fibronectin and β1 Integrin Receptors in the Binding of Mycobacterium leprae to NaSal Epithelial Cells

Byrd, Sally R.; Gelber, Robert H.; Bermudez, Luiz E.

doi:10.1006/clin.1993.1179

Cited by 29 publications

(27 citation statements)

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“…Nonetheless, M. leprae numbers inside RPMI 2650 cells doubled at 24 h of infection, suggesting a possible modulation of cell receptor expression. The capacity of M. leprae to interact with RPMI 2650 cells has been previously described (46). Interestingly, in a previous study, the percentage of M. leprae-infected A549 cells was similar to the percentage of cells infected with M. tuberculosis (54), suggesting that M. leprae is as efficient as M. tuberculosis at binding to and entering these cells.…”

Section: Discussionmentioning

confidence: 51%

“…A study using the nasal epithelial cell RPMI 2650 lineage showed that treatment with fibronectin increased M. leprae adherence to this cell. In addition, the ␤1 chain of integrins is also implicated in the binding of M. leprae to nasal epithelial cells (46). Several chaperones with potential adhesin properties were also found on the M. leprae surface ( Table 2).…”

Section: Resultsmentioning

confidence: 99%

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Interaction of Mycobacterium leprae with Human Airway Epithelial Cells: Adherence, Entry, Survival, and Identification of Potential Adhesins by Surface Proteome Analysis

et al. 2013

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f This study examined the in vitro interaction between Mycobacterium leprae, the causative agent of leprosy, and human alveolar and nasal epithelial cells, demonstrating that M. leprae can enter both cell types and that both are capable of sustaining bacterial survival. Moreover, delivery of M. leprae to the nasal septum of mice resulted in macrophage and epithelial cell infection in the lung tissue, sustaining the idea that the airways constitute an important M. leprae entry route into the human body. Since critical aspects in understanding the mechanisms of infection are the identification and characterization of the adhesins involved in pathogen-host cell interaction, the nude mouse-derived M. leprae cell surface-exposed proteome was studied to uncover potentially relevant adhesin candidates. A total of 279 cell surface-exposed proteins were identified based on selective biotinylation, streptavidin-affinity purification, and shotgun mass spectrometry; 11 of those proteins have been previously described as potential adhesins. In vitro assays with the recombinant forms of the histone-like protein (Hlp) and the heparin-binding hemagglutinin (HBHA), considered to be major mycobacterial adhesins, confirmed their capacity to promote bacterial attachment to epithelial cells. Taking our data together, they suggest that the airway epithelium may act as a reservoir and/or portal of entry for M. leprae in humans. Moreover, our report sheds light on the potentially critical adhesins involved in M. leprae-epithelial cell interaction that may be useful in designing more effective tools for leprosy control.

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Section: Discussionmentioning

confidence: 51%

Section: Resultsmentioning

confidence: 99%

Interaction of Mycobacterium leprae with Human Airway Epithelial Cells: Adherence, Entry, Survival, and Identification of Potential Adhesins by Surface Proteome Analysis

et al. 2013

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“…In vitro studies have shown that the attachment and the internalization of MAP by epithelial cells depend on the interaction between Fibronectin attachment proteins and fibronectin [68–70]. In fact β 1 integrins are the host cell receptors for fibronectin-opsonized mycobacteria [68, 71]. Because M-cells are the unique intestinal cells expressing β 1 integrins at a high density on their luminal surface, they represent the main entrance site for MAP [64].…”

Section: Development Architecture and Functions Of Peyer's Patchesmentioning

confidence: 99%

Peyer's Patches: The Immune Sensors of the Intestine

Jung

Hugot

Barreau

2010

International Journal of Inflammation

369

302

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The gut-associated lymphoid tissue (GALT) consists of isolated or aggregated lymphoid follicles forming Peyer's patches (PPs). By their ability to transport luminal antigens and bacteria, PPs can be considered as the immune sensors of the intestine. PPs functions like induction of immune tolerance or defense against pathogens result from the complex interplay between immune cells located in the lymphoid follicles and the follicle-associated epithelium. This crosstalk seems to be regulated by pathogen recognition receptors, especially Nod2. Although TLR exerts a limited role in PP homeotasis, Nod2 regulates the number, size, and T-cell composition of PPs, in response to the gut flora. In turn, CD4+ T-cells present in the PP are able to modulate the paracellular and transcellular permeabilities. Two human disorders, Crohn's disease and graft-versus-host disease are thought to be driven by an abnormal response toward the commensal flora. They have been associated with NOD2 mutations and PP dysfunction.

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“…This binding may involve fibronectin, a glycoprotein found in plasma and on the outer surface of many cell types (186). Similar to Mycobacterium leprae (32), M. tuberculosis may bind to epithelial cells since the bacterium produces and secretes the 30-to 31-kDa antigen 85 complex, a member of the fibronectin-binding protein family (246). In addition, a 28-kDa heparin-binding adhesin, produced by M. tuberculosis, will bind to sulfated glycoconjugates on host cells (136 (2).…”

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confidence: 99%