Sobre Mi:
I am a Senior Graduate Student at Ponce School of Medicine and a Medical Technologist with nine years of experience. My specialty in the PhD program is Immunochemistry and Molecular Genetics. My expertise is in the Development of Immunoassays and Protein Purification in the Asthma and Allergy fields and Cell and tissue cultures for the study of protein- protein interaction between bacteriophages and its bacterial host. My Thesis Project is to determine if the backside mutants of the tailspike protein (TSP) of the bacteriophage P22 causes defects in binding or hydrolysis of the LPS (lipopolysaccharide) at the cell membrane of its host Salmonella typhimurium. My career scope is to gather the necessary knowledge and experience to develop and establish a research career as a Scientist in the Public Health area of Infectious Diseases and Risk Assessment. This includes development of immunoassays and vaccines and characterization of key genes and proteins for correlation studies of diseases that are causing epidemic problems to the society (e.g. Infectious Diseases). I am in the best disposition to share knowledge and information with any fellow at the science community and to establish a collaborative relationship with anyone interested in my
Información de proyecto:
Our Lab studies are based on the study of the tailspike protein (TSP) of the bacteriophages P22 which infects Salmonella typhimurium and Є34 which infects Salmonella newington. We are focus in understanding the binding system of the virus to the outer membrane of there host. The phages use the TSP to hydrolyze the lipopolysaccharide (LPS) on the bacterial membrane in order to attach and introduce there genetic material and infect the host. We developed and cloned three mutants located in the backside of TSP and affect its binding. My project is to determine if the effect of these mutants is in the LPS binding or hydrolysis. The importance of this project is: 1- Understand how this virus attached permanently the membrane to infiltrate its DNA material and then create a way to mimic this mechanism synthetically to be use as therapeutic route in the treatment of these infections; 2- Understanding this protein- LPS interaction system will facilitate the studies of diseases and clinical conditions known to be due to defects in protein- protein interaction.