Costimulation Immunotherapy in Allergies and Asthma

Mir, Manzoor Ahmad

doi:10.1016/b978-0-12-802585-7.00004-2

Cited by 10 publications

(2 citation statements)

References 217 publications

(154 reference statements)

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“…Results also indicate that adjuvants derived from T-cells enhanced the efficacy of SLIT in a mouse model of asthma [226]. Other novel approaches to SLIT are said to have shown favourable results in mouse models when using genetically engineered hypoallergens [227]. In 2016, Ilaria used the TLR5 ligand (a fusion protein of flagellin) for intranasal and intraperitoneal inoculation of food allergy in mouse models, which decreased IgE production but did not lead to allergic sensitization [228].…”

Section: Recombinant Allergens In Animal Modelsmentioning

confidence: 99%

Egg Allergy: Diagnosis and Immunotherapy

Dona

Suphioglu

2020

IJMS

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Hypersensitivity or an allergy to chicken egg proteins is a predominant symptomatic condition affecting 1 in 20 children in Australia; however, an effective form of therapy has not yet been found. This occurs as the immune system of the allergic individual overreacts when in contact with egg allergens (egg proteins), triggering a complex immune response. The subsequent instantaneous inflammatory immune response is characterized by the excessive production of immunoglobulin E (IgE) antibody against the allergen, T-cell mediators and inflammation. Current allergen-specific approaches to egg allergy diagnosis and treatment lack consistency and therefore pose safety concerns among anaphylactic patients. Immunotherapy has thus far been found to be the most efficient way to treat and relieve symptoms, this includes oral immunotherapy (OIT) and sublingual immunotherapy (SLIT). A major limitation in immunotherapy, however, is the difficulty in preparing effective and safe extracts from natural allergen sources. Advances in molecular techniques allow for the production of safe and standardized recombinant and hypoallergenic egg variants by targeting the IgE-binding epitopes responsible for clinical allergic symptoms. Site-directed mutagenesis can be performed to create such safe hypoallergens for their potential use in future methods of immunotherapy, providing a feasible standardized therapeutic approach to target egg allergies safely.

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Section: Recombinant Allergens In Animal Modelsmentioning

confidence: 99%

Egg Allergy: Diagnosis and Immunotherapy

Dona

Suphioglu

2020

IJMS

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“…Mycobacteria have already developed intricate biosynthetic pathways that are well-organized and sustain their distinctive, thick cell walls, which help them retain cellular integrity, withstand stress and dormancy, and avoid detection by the immune system of the host. 10,11,[15][16][17][18] Moreover, most of the drug targets are proteins or enzymes that display a significant role during the various metabolic processes in Mtb, which prominently encompasses the biosynthesis of fatty acids, the process of translation, biosynthesis of the cell wall, the process of translation, as well as other molecular mechanisms essential for the survival of Mtb. 15 Decaprenylphosphoryl-β-D-ribose 2 ' -epimerase (DprE1) is a flavoenzyme playing a role in the biosynthesis of Mtb cell wall.…”

Section: Introductionmentioning

confidence: 99%

Computational Studies to Identify Potential Inhibitors Targeting the DprE1 Protein in Mycobacterium tuberculosis

Sheikh

Rizvi

et al. 2022

Int J. Pharm. Investigation

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Background: DprE1, which is a flavoenzyme, is very important for cell wall biosynthesis in Mycobacterium tuberculosis (Mtb) and for the pathogenesis, virulence, lethality, and stress resistance of the host. Drug-resistant tuberculosis is a challenging global human health issue, necessitating the development of novel, more effective treatment regimens without adverse effects. DprE1 represents a potential therapeutic target. It was explored as a drug target utilizing benzothiazoles (BTZ), which are enormously potential anti-bacterial agents and are currently being explored as anti-mycobacterial entities. Materials and Methods: We used virtual screening of bioactive molecules from PubChem and ZINC databases targeting DprE1, having bioactive thousands of molecules known for anti-microbial activity. In the present study, we selected 100 compounds as the most promising candidates to act as potential DprE1 inhibitors to control this emerging condition of tuberculosis infection. To identify the six topranked compounds, molecular docking was used to calculate the binding affinities (ranging from -8.3 to 10.0 kcal/mol) between various compounds (C1-C6) and the DprE1 protein.Results: Based on the results of an ADMET analysis, these six chemicals are safer potential drug candidates, as neither AMES toxicity nor carcinogenicity is present when toxicological properties are considered. Out of 6 compounds, the top-ranked compound exhibiting the best binding affinity against the drug target DprE1 (Pdb-id;4FEH) receptor was further subjected to molecular dynamic simulation for 100 nanoseconds to check the stability and trajectories by root-mean-square deviation (RMSD) and root-mean-square fluctuation (RMSF) graphs and interacting coordinates using Desmond Schrodinger Software. Conclusion: Our in-silico investigation identified potent inhibitors for the DprE1 protein of Mtb, and these compounds can be considered and recommended as the lead molecules in the treatment of tuberculosis.

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