By a News Reporter-Staff News Editor at Health & Medicine Week -- New research on Enzymes and Coenzymes is the subject of a report. According to news reporting out of Baltimore, Maryland, by NewsRx editors, research stated, "Gas vesicles are hollow, buoyant organelles bounded by a thin and extremely stable protein membrane. They are coded by a cluster of gvp genes in the halophilic archaeon, Halobacterium sp. NRC-1."
Our news journalists obtained a quote from the research from the University of Maryland School of Medicine, "Using an expression vector containing the entire gvp gene cluster, gas vesicle nanoparticles (GVNPs) have been successfully bioengineered for antigen display by constructing gene fusions between the gvpC gene and coding sequences from bacterial and viral pathogens. To improve and streamline the genetic system for bioengineering of GVNPs, we first constructed a strain of Halobacterium sp. NRC-1 deleted solely for the gvpC gene. The deleted strain contained smaller, more spindle-shaped nanoparticles observable by transmission electron microscopy, confirming a shape-determining role for GvpC in gas vesicle biogenesis. Next, we constructed expression plasmids containing N-terminal coding portions or the complete gvpC gene. After introducing the expression plasmids into the Halobacterium sp. NRC-1 ?gvpC strain, GvpC protein and variants were localized to the GVNPs by Western blotting analysis and their effects on increasing the size and shape of nanoparticles established by electron microscopy. Finally, a synthetic gene coding for Gaussia princeps luciferase was fused to the gvpC gene fragments on expression plasmids, resulting in an enzymatically active GvpC-luciferase fusion protein bound to the buoyant nanoparticles from Halobacterium. GvpC protein and its N-terminal fragments expressed from plasmid constructs complemented a Halobacterium sp. NRC-1 ?gvpC strain and bound to buoyant GVNPs. Fusion of the luciferase reporter gene from Gaussia princeps to the gvpC gene derivatives in expression plasmids produced GVNPs with enzymatically active luciferase bound."
According to the news editors, the research concluded: "These results establish a significantly improved genetic system for displaying foreign proteins on Halobacterium gas vesicles and extend the bioengineering potential of these novel nanoparticles to catalytically active enzymes."
For more information on this research see: An improved genetic system for bioengineering buoyant gas vesicle nanoparticles from Haloarchaea. Bmc Biotechnology, 2013;13():112. (BioMed Central - www.biomedcentral.com/; Bmc Biotechnology - www.biomedcentral.com/bmcbiotechnol/)
Our news journalists report that additional information may be obtained by contacting S. DasSarma, Institute of Marine and Environmental Technology and Dept. of Microbiology and Immunology, University of Maryland School of Medicine, 701 E Pratt Street, Baltimore, MD 21202, United States. Additional authors for this research include R. Karan, P. DasSarma, S. Barnes, F. Ekulona and B. Smith (see also Enzymes and Coenzymes).
Keywords for this news article include: Maryland, Genetics, Baltimore, Luciferases, Nanoparticle, United States, Nanotechnology, Oxidoreductases, Luminescent Proteins, Emerging Technologies, Enzymes and Coenzymes, North and Central America.
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