<?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%">Pastey, Manoj</style></author><author><style face="normal" font="default" size="100%">Samal, S K</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structure and sequence comparison of bovine respiratory syncytial virus fusion protein.</style></title><secondary-title><style face="normal" font="default" size="100%">Virus research</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Virus Res.</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%">Genes, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycosylation</style></keyword><keyword><style  face="normal" font="default" size="100%">HN Protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Processing, Post-Translational</style></keyword><keyword><style  face="normal" font="default" size="100%">Regulatory Sequences, Nucleic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Respiratory Syncytial Virus, Bovine</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Amino Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">Viral Envelope Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Viral Fusion Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Viral Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1993</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1993 Aug</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">29</style></volume><pages><style face="normal" font="default" size="100%">195-202</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The fusion (F) proteins of 10 strains of bovine respiratory syncytial virus (BRSV) were compared by radioimmunoprecipitation with fractionation on SDS-polyacrylamide gels. Two different molecular weights (15 kDa and 20 kDa) of the F2 proteins were demonstrated among the BRSV strains tested. To delineate the molecular basis for differences in the molecular weights of F2 subunits among the BRSV strains, the nucleotide sequences of the F genes of FS1 and VC464 strains were determined from cDNA clones. The deduced amino acid sequences were then compared to those of BRSV strains RB94, 391-2 and A51908. The F gene was highly conserved (&gt; 95%) among BRSV strains. Comparison of the deduced F2 amino acid sequences showed that the strain with F2 subunits of 20 kDa had three N-linked glycosylation sites, whereas the strains with F2 subunits of 15 kDa had two N-linked glycosylation sites. Analysis of F2 subunits in their deglycosylated forms indicated that the difference in the molecular weights of the F2 subunits was due to the difference in the extent of glycosylation.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8212860?dopt=Abstract</style></custom1></record></records></xml>