Elastin, a Novel Extracellular Matrix Protein Adhering to Mycobacterial Antigen 85 Complex

Kuo, C.J.; Ptak, Christopher; Hsieh, Ching-Lin; Akey, Bruce; Chang, Yung-Fu

doi:10.1074/jbc.m112.415679

Cited by 36 publications

(34 citation statements)

References 57 publications

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“…Consistent with the K D measured by SPR, K D of HTE20 binding to LigB12 was 0.97 ± 0.03 μM. This submicromolar affinity is comparable to the affinity of HTE27-28 binding to Ag85 (Kuo et al, 2013). Therefore, it is likely that the HTE-LigB interaction is physiological relevant, and HTE20 might potentially serve as adhesion blocker to diminish the leptospiral attachment to the host cell surface.…”

Section: Discussionsupporting

confidence: 80%

Leptospira Immunoglobulin-Like Protein B Interacts with the 20th Exon of Human Tropoelastin Contributing to Leptospiral Adhesion to Human Lung Cells

Hsieh

Tseng

et al. 2017

Front. Cell. Infect. Microbiol.

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Leptospira immunoglobulin-like protein B (LigB), a surface adhesin, is capable of mediating the attachment of pathogenic leptospira to the host through interaction with various components of the extracellular matrix (ECM). Human tropoelastin (HTE), the building block of elastin, confers resilience and elasticity to lung, and other tissues. Previously identified Ig-like domains of LigB, including LigB4 and LigB12, bind to HTE, which is likely to promote Leptospira adhesion to lung tissue. However, the molecular mechanism that mediates the LigB-HTE interaction is unclear. In this study, the LigB-binding site on HTE was further pinpointed to a N-terminal region of the 20th exon of HTE (HTE20N). Alanine mutants of basic and aromatic residues on HTE20N significantly reduced binding to the LigB. Additionally, HTE-binding site was narrowed down to the first β-sheet of LigB12. On this binding surface, residues F1054, D1061, A1065, and D1066 were critical for the association with HTE. Most importantly, the recombinant HTE truncates could diminish the binding of LigB to human lung fibroblasts (WI-38) by 68%, and could block the association of LigA-expressing L. biflexa to lung cells by 61%. These findings should expand our understanding of leptospiral pathogenesis, particularly in pulmonary manifestations of leptospirosis.

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Section: Discussionsupporting

confidence: 80%

Leptospira Immunoglobulin-Like Protein B Interacts with the 20th Exon of Human Tropoelastin Contributing to Leptospiral Adhesion to Human Lung Cells

Hsieh

Tseng

et al. 2017

Front. Cell. Infect. Microbiol.

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“…Although never demonstrated, they could also potentially be present in the periplasmic compartment (between the inner membrane and the mycomembrane) either on the way to the mycomembrane or as their final destination. They could also directly interact with the AG or PG as it has been proposed (but not experimentally tested) for all cMytA-like proteins through their LGFP repeat-containing C-terminal domain (26) (74). As such, they are involved in the interaction with the host extracellular matrix and in the pathogenicity of the bacterium.…”

Section: Localization Of Mycoloyltransferases In the Cellmentioning

confidence: 93%

Mycoloyltransferases: A large and major family of enzymes shaping the cell envelope of Corynebacteriales

Dautin

Silva

Constantinesco-Becker

et al. 2017

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…ATIIs express a variety of molecules that have been shown to participate in receptor-mediated endocytosis following recognition of M.tb antigens, such as integrins [6], carbohydrate receptors and extracellular matrix (ECM) components [40][41] [42;43], and pattern recognition receptors (PRRs) [6]. Integrins, including CD51 (vitronectin) and CD29 (β1 integrin), have been shown to synergize and be involved in M.tb invasion [6].…”

Section: Mtb Binding and Invasion Of The Alveolar Epitheliummentioning

confidence: 99%

Alveolar Epithelial Cells in <b><i>Mycobacterium tuberculosis</i></b> Infection: Active Players or Innocent Bystanders?

Scordo

Knoell²,

Torrelles

2015

J Innate Immun

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Tuberculosis (TB) is a disease that kills one person every 18 s. TB remains a global threat due to the emergence of drug-resistant Mycobacterium tuberculosis (M.tb) strains and the lack of an efficient vaccine. The ability of M.tb to persist in latency, evade recognition following seroconversion, and establish resistance in vulnerable populations warrants closer examination. Past and current research has primarily focused on examination of the role of alveolar macrophages and dendritic cells during M.tb infection, which are critical in the establishment of the host response during infection. However, emerging evidence indicates that the alveolar epithelium is a harbor for M.tb and critical during progression to active disease. Here we evaluate the relatively unexplored role of the alveolar epithelium as a reservoir and also its capacity to secrete soluble mediators upon M.tb exposure, which influence the extent of infection. We further discuss how the M.tb-alveolar epithelium interaction instigates cell-to-cell crosstalk that regulates the immune balance between a proinflammatory and an immunoregulatory state, thereby prohibiting or allowing the establishment of infection. We propose that consideration of alveolar epithelia provides a more comprehensive understanding of the lung environment in vivo in the context of host defense against M.tb.

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Elastin, a Novel Extracellular Matrix Protein Adhering to Mycobacterial Antigen 85 Complex

Cited by 36 publications

References 57 publications

Leptospira Immunoglobulin-Like Protein B Interacts with the 20th Exon of Human Tropoelastin Contributing to Leptospiral Adhesion to Human Lung Cells

Leptospira Immunoglobulin-Like Protein B Interacts with the 20th Exon of Human Tropoelastin Contributing to Leptospiral Adhesion to Human Lung Cells

Mycoloyltransferases: A large and major family of enzymes shaping the cell envelope of Corynebacteriales

Alveolar Epithelial Cells in <b><i>Mycobacterium tuberculosis</i></b> Infection: Active Players or Innocent Bystanders?

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