Extracellular vesicles (EVs) are nano-sized lipid-bilayer encapsulated vesicles produced by the cells. These EVs are released into the surrounding space by almost all cell types. The EVs help in intercellular communication via their payloads which contain various proteins, lipids, and nucleic acids generated from the donor cells and allow for synergistic responses in surrounding cells. In recent years, EVs have been increasingly important in treating infectious diseases, including respiratory tract infections, urinary tract infections, wound infections, sepsis, and intestinal infections. Studies have confirmed the therapeutic value of mesenchymal stem cell-derived EVs (MSC-EVs) for treating infectious diseases to eliminate the pathogen, modulate the resistance, and restore tissue damage in infectious diseases. This can be achieved by producing antimicrobial substances, inhibiting pathogen multiplication, and activating macrophage phagocytic activity. Pathogen compounds can be diffused by inserting them into EVs produced and secreted by host cells or by secreting them as microbial cells producing EVs carrying signalling molecules and DNA shielding infected pathogens from immune attack. EVs play a key role in infectious pathogenesis and hold great promise for developing innovative treatments. In this review, we discuss the role of MSC-EVs in treating various infectious diseases.
Background
Lysyl oxidase is an extracellular regulatory enzyme with an imperative role in interlinking of collagen and elastin by oxidizing lysine residues. Lysyl oxidase has been implicated in incidence of mammary tumors in bitches. Therefore, it becomes significant to study the structural and functional features of this enzyme for a better understanding of its molecular mechanisms.
Results
The detailed computational investigation of the canine lysyl oxidase protein was analyzed in silico with respect to its physicochemical properties, secondary and tertiary structure predictions and functional analysis using standard bioinformatic tools. Lysyl oxidase is a flexible protein with an average molecular weight of around 46 kDa, unstable, hydrophilic, and extracellular (secretory) in nature. Twelve cysteine residues and a disulfide bridge were also found. Secondary structure analysis shows that most of the protein has predominant coiled configuration. A putative copper-binding region signature was predicted. The phylogenetic relationship of canine lysyl oxidase with a vast range of mammalian species indicates that the protein was very well conserved throughout the course of evolution. Top 10 interacting proteins were identified using STRING v10.0 analysis, elastin being the closest interacting protein. Functional analysis by InterproScan predicted protein’s biological role in oxidation-reduction process.
Conclusion
Understanding the structural and functional properties of the protein will facilitate a better understanding of its mechanism of enzyme action. Further, the predicted 3D model will serve as a cornerstone for further understanding towards the tumorigenesis potential of the protein.
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