RT Journal Article SR Electronic(1) A1 García-Barreno, Blanca A1 Steel, John A1 Payá, Monica A1 Martínez-Sobrido, Luis A1 Delgado, Teresa A1 Yeo, Robert P. A1 Melero, José A.YR 2005 T1 Epitope mapping of human respiratory syncytial virus 22K transcription antitermination factor: role of N-terminal sequences in protein folding JF Journal of General Virology, VO 86 IS 4 SP 1103 OP 1107 DO https://doi.org/10.1099/vir.0.80712-0 PB Microbiology Society, SN 1465-2099, AB The reactivity of a panel of 12 monoclonal antibodies raised against the human respiratory syncytial virus 22 kDa (22K) protein was tested by Western blotting with a set of 22K deletion mutants. The results obtained identified sequences in the C-terminal half of the 22K polypeptide required for integrity of most antibody epitopes, except for epitope 112, which was lost in mutants with short N-terminal deletions. This antibody, in contrast to the others, failed to immunoprecipitate the native 22K protein, indicating that the N terminus of this protein is buried in the native molecule and exposed only under the denaturing conditions of Western blotting. In addition, N-terminal deletions that abolished reactivity with monoclonal antibody 112 also inhibited phosphorylation of the 22K protein previously identified at Ser-58 and Ser-61, suggesting that the N terminus is important in regulating the 22K protein phosphorylation status, most likely as a result of its requirement for protein folding., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.80712-0