| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Servicio Virologia, Centro Nacional de Microbiología, Virología e Immunología Sanitarias, Instituto de Salud Carlos III, Majadahonda, 28220 Madrid
and2 Servicio Virologia, Centro Nacional de Microbiología, Virología e Immunología Sanitarias, Instituto de Salud Carlos III, Majadahonda, 28220 Madrid, Spain
The phosphoprotein (P protein) from human respiratory syncytial virus Long strain, labelled in vivo with [32P]orthophosphate, was purified from virions or virus-infected human epithelial (Hep-2) cells. The main phosphorylated amino acid found was serine. The determination of the N-terminal sequence of unphosphorylated and phosphorylated fragments of P protein obtained after chemical or enzymic treatments suggested that some or all of the six serines present at positions 116, 117, 119, 143, 156 and 161 are the major phosphorylated residues, although a modification in serine residues at positions 86, 94 and 99 can not be ruled out.
Received 20 June 1990;
accepted 13 February 1991.
This article has been cited by other articles:
|
|
 |
|
  M. Sun, S. M. Fuentes, K. Timani, D. Sun, C. Murphy, Y. Lin, A. August, M. N. Teng, and B. He Akt Plays a Critical Role in Replication of Nonsegmented Negative-Stranded RNA Viruses J. Virol., January 1, 2008; 82(1): 105 - 114. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Schmid, D. Mayer, U. Schneider, and M. Schwemmle Functional Characterization of the Major and Minor Phosphorylation Sites of the P Protein of Borna Disease Virus J. Virol., June 1, 2007; 81(11): 5497 - 5507. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T.-L. Tran, N. Castagne, D. Bhella, P. F. Varela, J. Bernard, S. Chilmonczyk, S. Berkenkamp, V. Benhamo, K. Grznarova, J. Grosclaude, et al. The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer J. Gen. Virol., January 1, 2007; 88(1): 196 - 206. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Asenjo, E. Calvo, and N. Villanueva Phosphorylation of human respiratory syncytial virus P protein at threonine 108 controls its interaction with the M2-1 protein in the viral RNA polymerase complex J. Gen. Virol., December 1, 2006; 87(12): 3637 - 3642. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. T. Llorente, B. Garcia-Barreno, M. Calero, E. Camafeita, J. A. Lopez, S. Longhi, F. Ferron, P. F. Varela, and J. A. Melero Structural analysis of the human respiratory syncytial virus phosphoprotein: characterization of an {alpha}-helical domain involved in oligomerization J. Gen. Virol., January 1, 2006; 87(1): 159 - 169. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Asenjo, L. Rodriguez, and N. Villanueva Determination of phosphorylated residues from human respiratory syncytial virus P protein that are dynamically dephosphorylated by cellular phosphatases: a possible role for serine 54 J. Gen. Virol., April 1, 2005; 86(4): 1109 - 1120. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Castagne, A. Barbier, J. Bernard, H. Rezaei, J.-C. Huet, C. Henry, B. D. Costa, and J.-F. Eleouet Biochemical characterization of the respiratory syncytial virus P-P and P-N protein complexes and localization of the P protein oligomerization domain J. Gen. Virol., June 1, 2004; 85(6): 1643 - 1653. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. Lu, C.-H. Ma, R. Brazas, and H. Jin The Major Phosphorylation Sites of the Respiratory Syncytial Virus Phosphoprotein Are Dispensable for Virus Replication In Vitro J. Virol., October 2, 2002; 76(21): 10776 - 10784. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Villanueva, R. Hardy, A. Asenjo, Q. Yu, and G. Wertz The bulk of the phosphorylation of human respiratory syncytial virus phosphoprotein is not essential but modulates viral RNA transcription and replication J. Gen. Virol., January 1, 2000; 81(1): 129 - 133. [Abstract] [Full Text]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
