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Journal ArticleDOI

Enolase of Mycobacterium tuberculosis is a surface exposed plasminogen binding protein.

TLDR
It is shown here that Mtb enolase is a surface exposed plasminogen binding protein which upon immunization confers significant protection against Mtb challenge.
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This article is published in Biochimica et Biophysica Acta.The article was published on 2017-01-01. It has received 31 citations till now. The article focuses on the topics: Enolase & Plasmin.

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Citations
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Bacterial Excretion of Cytoplasmic Proteins (ECP): Occurrence, Mechanism, and Function.

TL;DR: The excretion of cytoplasmic and signal-peptide-less proteins (ECP) by microorganisms and eukaryotes remains a fascinating topic and some CPs might be promising candidates for vaccine developments against major bacterial pathogens.
Journal ArticleDOI

Plasminogen-binding proteins as an evasion mechanism of the host's innate immunity in infectious diseases.

TL;DR: A new picture is starting to arise about how this glycolytic enzyme could acquire an entirely new role as modulator of the innate immune system in the context of the host–parasite relationship.
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TrmFO, a Fibronectin-Binding Adhesin of Mycoplasma bovis

TL;DR: This is the first report to characterize the Fn-binding ability of TrmFO and its role in the bacterial adhesion to host cells, and it is found that rTrmFO bound Fn in a dose-dependent manner.
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The Complement Binding and Inhibitory Protein CbiA of Borrelia miyamotoi Degrades Extracellular Matrix Components by Interacting with Plasmin(ogen).

TL;DR: A surface-exposed molecule, CbiA exhibiting complement binding and inhibitory capacity and rendering spirochetes resistant to complement-mediated lysis is identified, appearing to play a crucial role in the protein-protein interaction as binding of plasminogen was inhibited by the lysine analog tranexamic acid as well as increasing ionic strength.
References
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Journal ArticleDOI

Bio3d: an R package for the comparative analysis of protein structures

TL;DR: An automated procedure for the analysis of homologous protein structures has been developed that facilitates the characterization of internal conformational differences and inter-conformer relationships and provides a framework for theAnalysis of protein structural evolution.
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Multifunctional alpha-enolase: its role in diseases.

TL;DR: Enolase is a multifunctional protein, and its ability to serve as a plasminogen receptor on the surface of a variety of hematopoetic, epithelial and endothelial cells suggests that it may play an important role in the intravascular and pericellular fibrinolytic system.
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Non-classical protein secretion in bacteria.

TL;DR: Predicting of disorder reveals that bacterial secretory proteins are more structurally disordered than their cytoplasmic counterparts, thus allowing for the identification of novel non-classically secreted proteins.
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Mycobacterial cell wall: Structure and role in natural resistance to antibiotics

TL;DR: The cell wall barrier alone cannot produce significant levels of drug resistance, which requires synergistic contribution from a second factor, such as the enzymatic inactivation of drugs.
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α-Enolase, a Novel Strong Plasmin(ogen) Binding Protein on the Surface of Pathogenic Streptococci

TL;DR: These findings, showing both the protected protease activity of SEN-bound plasmin and SEN-specific immune responses, provide evidence for an important role of SEN in the disease process and post-streptococcal autoimmune diseases.
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