No abstract
Screening of HLA class II epitope-based peptides as potential vaccine candidates is one of the most rational approach for vaccine development against Hendra virus (HeV) infection, for which currently there is no successful vaccine in practice. In this study, screening of epitopes from HeV proteins viz matrix, glycoprotein, nucleocapsid, fusion, C protein, V protein, W protein and polymerase, followed by highest binding affinity & molecular dynamic simulation of selected T-cell epitopes with their corresponding HLA class II alleles has been done. The server ProPred facilitates the binding prediction of HLA class II allele specific epitopes from the antigenic protein sequences of HeV. PEPstrMOD server was used for PDB structure modeling of the screened epitopes and MODELLER was used for HLA alleles modeling. We docked the selected T-cell epitopes with their corresponding HLA allele structures using the AutoDock 4.2 tool. Further the selected docked complex structures were optimized by NAnoscale Molecular Dynamics program (NAMD) at 5 ps, with the CHARMM-22 force field parameter incorporated in Visual Molecular Dynamics (VMD 1.9.2) and complex structure stability was evaluated by calculating RMSD values. Epitopes IRIFVPATN (Nucleocapsid), MRNLLSQSL (Nucleocapsid), VRRAGKYYS (Matrix) and VRLKCLLCG (Fusion) proteins have shown considerable binding with DRB1*0806, DRB1*1304, DRB1*0701 and DRB1*0301 HLA class II allele respectively. Toxicity, antigenicity and population coverage of epitopes IRIFVPATN, MRNLLSQSL, VRRAGKYYS and VRLKCLLCG were analyzed by Toxin Pred, Vexijen and IEDB tool, respectively. The potential T-cell epitopes can be utilized in designing comprehensive epitope-based vaccines and diagnostic kits against Hendra virus after further in-vivo studies.
Interaction of [MoO 2 (acac) 2 ] with internally functionalized oximes like HON=C(CH 3 )Ar (Ar = C 4 H 3 S, C 4 H 3 O or C 5 H 4 N) and Schiff's Bases derived from β – diketones like HOC(R)CHC(R′)=NC 6 H 5 (R = R’ = CH 3 or C 6 H 5 ; R = CH 3 and R’ = C 6 H 5 ) led to the formation of yellow dioxomolybdenum(VI) complexes of the type [MoO 2 {ON=C(CH 3 )Ar} 2 ] and [MoO 2 {OC(R)CHC(R′)=NC 6 H 5 } 2 ]. Oximes were synthesized by green methodology. The newly synthesized complexes were characterized on basis of elemental analysis and various spectral findings. Anticandidal activity of [MoO 2 {ON=C(CH 3 )C 6 H 4 N} 2 ] clearly reveals that the complex is biologically active against fungal diseases.
L-asparaginase is a valuable protein therapeutic drug utilized for the treatment of leukemia and lymphomas. Administration of asparaginase leads to asparagine starvation causing inhibition of protein synthesis, growth, and proliferation of tumor cells. Besides its clinical significance, the enzyme also finds application in the food sector for mitigation of a cancer-causing agent acrylamide. The numerous applications ensue huge market demands and create a continued interest in the production of costeffective, more specific, less immunogenic and stable formulations which can cater both the clinical and food processing requirements. The current review article approaches the process parameters of submerged and solid-state fermentation strategies for the microbial production of the L-asparaginase from diverse sources, genetic engineering approaches used for the production of L-asparaginase enzyme and major applications in clinical and food sectors. The review also addresses the immunological issues associated with the L-asparaginase usage and the immobilization strategies, drug delivery systems employed to circumvent the toxicity complications are also discussed. The future prospects for microbial Lasparaginase production are discussed at the end of the review article.
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