Infection by H1N1 flu virus revealing T-cell acute lymphoid leukaemia: about two cases

Lefèvre, Guillaume; Ianotto, Jean‐Christophe; Tempescul, Adrian; Lemoine, Philippe; Guillerm, Gaëlle; Berthou, Christian

doi:10.1007/s00277-010-1132-9

Cited by 2 publications

(1 citation statement)

References 7 publications

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“…Among the above-identified non-metals compatible for binding with Asp proteins, Cef is known to be a β-lactam antibiotic with application in treating pneumonia [43] and also effective when provided to cancer patients to treat urinary tract infection, septicemia as per Rolston and team [44]. The antibiotic Cefotaxime in combination with Ciprofloxacin and Ofloxacin is reportedly found to be used in the treatment of neutropenia among cancer patients [45,46]. The studies revealed that Cefotaxime is prescribed to all age groups including neonates [47].…”

Section: Analysis Of Asp Protein By Galaxysite Toolmentioning

confidence: 99%

Structural Determination of L-Asparaginase Ii of Streptomyces Albidoflavus and Interaction Analysis With L-Asparagine and Cefotaxime

TEJASWINI

Malothu

2021

Int J App Pharm

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Objective: L-Asparaginase enzyme possesses a crucial role in the treatment of various hematologic malignancies. The current study focuses on homology modeling and interaction analysis of L-Asparaginase proteins belonging to Streptomyces albidoflavus (S. albidoflavus) with the essential ligand L-Asparagine and subsequent analysis with essential β-lactam antibiotic Cefotaxime. Methods: The process of understanding Asparaginase interactions primarily involved structure determination of WP_096097608, WP_095730301, which is achieved by GalaxyTBM, I-TASSER and SWISS-MODEL. Further, the S. albidoflavus Asparaginase proteins are subjected to GalaxySite and Autodock Vina of PyRx analysis. Results: The GalaxyTBM predicted structures of both the proteins are found promising on various validation studies. The two Asparaginase proteins exhibited high binding affinities of-6.8 and-6.5 kcal/mol with Cefotaxime and-5.1 and-4.9 kcal/mol towards Asparagine. The protein WP_096097608 residues forming hydrogen bonds with L-Asparagine are also analysed to involve in interaction with Cefotaxime on individual docking analysis. Conclusion: The current findings details the two S. albidoflavus Asparaginase proteins affinity towards L-Asparagine, hence can be assessed further for immunogenicity studies. In addition to the above findings, an attempt is made to find the L-Asparaginase binding possibilities with non-metals that identified an essential β-lactam antibiotic Cefotaxime to be an effective inhibitor. This study helps in understanding the interactions of L-Asparaginase with Cefotaxime, as intake of antibiotics between the phases of chemotherapy is observed to treat various infections and also as an antibiotic to microbes that utilize Asparaginase as a vital enzyme.

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