Browsing by Author "Lim T.S."
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Publication Cloning, expression, and purification of the hemolysin/cytolysin (HlyE antigen) from Salmonella enterica serovar Typhi: Potential application for immunoassay development(Elsevier Inc., 2013) ;Ong E.B.B. ;Anthony A.A. ;Ismail A. ;Ismail A. ;Lim T.S. ;Chancellory Building ;Universiti Sains Malaysia (USM)Universiti Sains Islam Malaysia (USIM)The hemolysin (HlyE) protein of Salmonella enterica serovar Typhi was reported to be antigenic. This work describes the cloning, expression, and purification of a hexahistidine-tagged HlyE protein under native conditions. Immunoblot analysis and a competitive enzyme-linked immunosorbent assay using sera from typhoid patients showed the presence of HlyE-specific antibodies in circulation. � 2013 Elsevier Inc. - Some of the metrics are blocked by yourconsent settings
Publication Phage display antibodies for diagnostic applications(2013) ;Hairul Bahara N.H. ;Tye G.J. ;Choong Y.S. ;Ong E.B.B. ;Ismail A. ;Lim T.S. ;Universiti Sains Malaysia (USM)Universiti Sains Islam Malaysia (USIM)With major developments in molecular biology, numerous display technologies have been successfully introduced for recombinant antibody production. Even so, phage display still remains the gold standard for recombinant antibody production. Its success is mainly attributed to the robust nature of phage particles allowing for automation and adaptation to modifications. The generation of monospecific binders provides a vital tool for diagnostics at a lower cost and higher efficiency. The flexibility to modify recombinant antibodies allows great applicability to various platforms for use. This review presents phage display technology, application and modifications of recombinant antibodies for diagnostics. � 2013 The International Alliance for Biological Standardization. - Some of the metrics are blocked by yourconsent settings
Publication Salmonella Typhi TolC protein: A molecular dynamics investigation(2014) ;Leong W. ;Lim T.S. ;Ismail A. ;Choong Y.S. ;Islamic Science Institute ;Universiti Sains Malaysia (USM)Universiti Sains Islam Malaysia (USIM)Introduction: The TolC family of proteins of Escherichia coli and other pathogenic Gram negative bacteria plays an important role as an outer membrane channel for the expulsion of drug and toxin from the cell. Typhoid fever, caused by Salmonella enterica serovar Typhi kills more than 200 000 lives annually. In S. Typhi, a TolC outer membrane protein was found to be antigenic for this pathogen. Understanding the dynamics of the S. Typhi TolC protein is essential towards development of diagnostics, therapeutics and vaccine towards typhoid fever. Therefore, molecular dynamics simulation has been performed on the protein. Objective: To refine homology structure of S. Typhi TolC protein by molecular dynamics simulation. Methods: A homology model of the S. Typhi TolC protein was embedded in phosphatidylethanolamine lipid bilayer. Water molecules were added and the system was subsequently neutralized. Minimization was performed by steepest descent method following which; temperature was equilibrated at 310.15K in the NVT ensemble. A 1 ns NPT run was performed with restraint on protein atoms to maintain pressure at 1 bar. Finally, production simulation was performed for 20 ns without restraints in the NPT ensemble. The average structure of the protein was generated by RMS fitting of all protein atoms from the production run and averaging over the coordinates. Results & Discussion: Results showed that the membrane simulation was energetically stable and reproduced experimental value. The protein conformation was also stable in simulation. Conformational analysis showed that the protein is highly mobile at the extracellular loops and periplasmic helices region. From Ramachandran plot and Errat analysis, the average structure showed improvements over the initial model. Conclusion: The average structure could be advantageous in aiding design efforts for inhibitors and binders against the S. Typhi TolC protein. � 2014 Asian Pacific Tropical Medicine Press.