Syed Hussain Mir (PhD)

Assistant Professor

Clinical Biochjemistry

University of Kashmir 

 

 

      

   

Research Interest:

Engineering of filamentous phages & Development of recombinant monoclonal antibodies by phage display for generation of therapeutic and diagnostic tools.

The research interests of my laboratory are protein engineering and development of recombinant monoclonal antibody fragments for therapeutic and clinical diagnostic purposes. We use the molecular biology techniques and Phage Display approach to engineer and develop the molecular libraries of antibody fragments and random peptides. These libraries are used as the source for expression and isolation of useful binders against various therapeutically important protein targets. The PI (principal investigator) is an expert in the generation of recombinant antibody fragment libraries in filamentous phage vectors. The germ-line VH and VL gene pools from immunized and non-immunized sources are used to construct these molecular diversity libraries.

 Recombinant Antibodies

   

       

Filamentous phages (EM image)

    

          

      

Monovalent phage display

       

      

Generation of avian monoclonal antibody fragments for structural & biochemical characterization of difficult membrane proteins.

Membrane proteins are challenging targets for crystallization and structure determination by X-ray crystallography. Antibody mediated crystallization has a major impact on the advancing structural and functional characterization of difficult membrane proteins. The limited availability of suitable hybridoma cell lines due to low immunogenicity of therapeutically important human membrane proteins in mice has impeded the high-throughput application of this approach. Therefore, our group employs an efficient method to obtain high affinity binders against difficult targets by phage display exploiting the avian immune system. The recombinant chicken antibodies are generated against many membrane transporter proteins, GTP binding proteins and other difficult targets. Some of these antibody fragments are used for structural characterization.