<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Dolan, Brian P</style></author><author><style face="normal" font="default" size="100%">Li, Lily</style></author><author><style face="normal" font="default" size="100%">Takeda, Kazuyo</style></author><author><style face="normal" font="default" size="100%">Bennink, Jack R</style></author><author><style face="normal" font="default" size="100%">Yewdell, Jonathan W</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Defective ribosomal products are the major source of antigenic peptides endogenously generated from influenza A virus neuraminidase.</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of immunology (Baltimore, Md. : 1950)</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Immunol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigen Presentation</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigens, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Dendritic Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Dogs</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Activation</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Stability</style></keyword><keyword><style  face="normal" font="default" size="100%">Epitopes</style></keyword><keyword><style  face="normal" font="default" size="100%">Fibroblasts</style></keyword><keyword><style  face="normal" font="default" size="100%">H-2 Antigens</style></keyword><keyword><style  face="normal" font="default" size="100%">Influenza A Virus, H1N1 Subtype</style></keyword><keyword><style  face="normal" font="default" size="100%">L Cells (Cell Line)</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Monocytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Neuraminidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Orthomyxoviridae Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Ovalbumin</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptide Fragments</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Biosynthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Folding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Ribosomal Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2010 Feb 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">184</style></volume><pages><style face="normal" font="default" size="100%">1419-24</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The defective ribosomal product (DRiP) hypothesis of endogenous Ag processing posits that rapidly degraded forms of nascent proteins are a major source of peptide ligands for MHC class I molecules. Although there is broad experimental support for the DRiP hypothesis, careful kinetic analysis of the generation of defined peptide class I complexes has been limited to studies of recombinant vaccinia viruses expressing genes derived from other organisms. In this study, we show that insertion of the SIINFEKL peptide into the stalk of influenza A virus neuraminidase (NA) does not detectably modify NA folding, degradation, transport, or sp. act. when expressed in its natural context of influenza A virus infection. Using the 25-D1.16 mAb specific for K(b)-SIINFEKL to precisely quantitate cell surface complexes by flow cytometry, we demonstrate that SIINFEKL is generated in complete lockstep with initiation and abrogation of NA biosynthesis in both L-K(b) fibroblast cells and DC2.4 dendritic/monocyte cells. SIINFEKL presentation requires active proteasomes and TAP, consistent with its generation from a cytosolic DRiP pool. From the difference in the shutoff kinetics of K(b)-SIINFEKL complex expression following protein synthesis versus proteasome inhibition, we estimate that the t(1/2) of the biosynthetic source of NA peptide is approximately 5 min. These observations extend the relevance of the DRiP hypothesis to viral proteins generated in their natural context.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/20038640?dopt=Abstract</style></custom1></record></records></xml>