By a News Reporter-Staff News Editor at Gene Therapy Weekly -- New research on Peptides and Proteins is the subject of a report. According to news reporting originating in La Jolla, California, by NewsRx journalists, research stated, "Adenoviruses (AdV) are broadly employed as gene delivery vectors. Copy numbers of all AdV proteins were measured, and the release of proteins upon heat stress investigated."
The news reporters obtained a quote from the research from Scripps Research Institute, "The viral protease plays a distinct role in the segmented release of AdV proteins. Our characterization by mass spectrometry provides new insight in HAdV disassembly during entry into host cells. Using high-resolution MS-based proteomics in combination with multiple protease digestion, we profiled, with on average 90% sequence coverage, all 13 viral proteins present in an human adenovirus (HAdV) vector. This in-depth profile provided multiple peptide-based evidence on intrinsic protease activity affecting several HAdV proteins. Next, the generated peptide library was used to develop a targeted proteomics method using selected reaction monitoring (SRM) aimed at quantitative profiling of the stoichiometry of all 13 proteins present in the HAdV. We also used this method to probe the release of specific virus proteins initiated by thermal stimulation, mimicking the early stage of HAdV disassembly during entry into host cells. We confirmed the copy numbers of the most well characterized viral capsid components and established the copy numbers for proteins whose stoichiometry has so far not been accurately defined. We also found that heating HAdV induces the complete release of the penton base and fiber proteins as well as a substantial release of protein VIII and VI. For these latter proteins, maturational proteolysis by the adenoviral protease leads to the differential release of fragments with certain peptides being fully released and others largely retained in the AdV particles."
According to the news reporters, the research concluded: "This information is likely to be beneficial for the ongoing interpretation of high resolution cryoEM and x-ray electron density maps."
For more information on this research see: Adenovirus Composition, Proteolysis, and Disassembly Studied by In-depth Qualitative and Quantitative Proteomics. Journal of Biological Chemistry, 2014;289(16):11421-11430. Journal of Biological Chemistry can be contacted at: Amer Soc Biochemistry Molecular Biology Inc, 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)
Our news correspondents report that additional information may be obtained by contacting M. Benevento, Scripps Res Inst, Dept. of Integrat Struct & Computat Biol, La Jolla, CA 92037, United States. Additional authors for this research include S. Di Palma, J. Snijder, C.L. Moyer, V.S. Reddy, G.R. Nemerow and A.J.R. Heck (see also Peptides and Proteins).
Keywords for this news article include: Biotechnology, Viral, La Jolla, Genetics, Genomics, Protease, California, Adenovirus, Proteomics, Amino Acids, Gene Therapy, United States, Bioengineering, Peptide Libraries, Enzymes and Coenzymes, Peptides and Proteins, North and Central America
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