| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Servicio de Virología, Centro Nacional de Microbiología, Virología e Inmunología Sanitarias, Instituto de Salud Carlos III, Majadahonda 28220 Madrid
and2 Servicío de Endocrinología, Hospital Ramón y Cajal, Madrid 28034, Spain
P protein, the structural phosphoprotein of the Long strain of respiratory syncytial (RS) virus, is phosphorylated at serine residues. Some of these residues are candidates for modification by casein kinase II, as they are contained in consensus sequences. A cellular protein kinase, able to phosphorylate the P protein in vitro and apparently associated with purified RS virions, has been partially purified from HEp-2 cells. It shows several characteristics similar to those of casein kinase II. The P protein is modified in vitro by this activity mainly at serine residues located near the C terminus, which are also modified during virus infection. Thus, the P protein is phosphorylated in vivo in two regions, a central region as previously described, and another located in the C-terminal part of the molecule. The protein kinase involved in the phosphorylation of the C-terminal domain is similar to a cellular casein kinase II.
Received 18 August 1993;
accepted 8 October 1993.
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]
|
|
|
|
 |
|
 G. Betser-Cohen, G. Katz, T. Gonen-Gross, N. Stern, T. I. Arnon, H. Achdout, R. Gazit, and O. Mandelboim Reduced KIR2DL1 Recognition of MHC Class I Molecules Presenting Phosphorylated Peptides. J. Immunol., June 1, 2006; 176(11): 6762 - 6769. [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]
|
|
|
|
|
|
L. Rodriguez, I. Cuesta, A. Asenjo, and N. Villanueva Human respiratory syncytial virus matrix protein is an RNA-binding protein: binding properties, location and identity of the RNA contact residues J. Gen. Virol., March 1, 2004; 85(3): 709 - 719. [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]
|
|
|
|
|
|
I. Cuesta, X. Geng, A. Asenjo, and N. Villanueva Structural Phosphoprotein M2-1 of the Human Respiratory Syncytial Virus Is an RNA Binding Protein J. Virol., November 1, 2000; 74(21): 9858 - 9867. [Abstract] [Full Text]
|
|
|
|
|
|
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]
|
|
|
|
 |
|
 T. Ogino, M. Iwama, J. Kinouchi, Y. Shibagaki, T. Tsukamoto, and K. Mizumoto Involvement of a Cellular Glycolytic Enzyme, Phosphoglycerate Kinase, in Sendai Virus Transcription J. Biol. Chem., December 10, 1999; 274(50): 35999 - 36008. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. N. Hwang, N. Englund, T. Das, A. K. Banerjee, and A. K. Pattnaik Optimal Replication Activity of Vesicular Stomatitis Virus RNA Polymerase Requires Phosphorylation of a Residue(s) at Carboxy-Terminal Domain II of Its Accessory Subunit, Phosphoprotein P J. Virol., July 1, 1999; 73(7): 5613 - 5620. [Abstract] [Full Text]
|
|
|
|
|
|
C. C. Huntley, B. P. De, and A. K. Banerjee Phosphorylation of Sendai Virus Phosphoprotein by Cellular Protein Kinase C zeta J. Biol. Chem., June 27, 1997; 272(26): 16578 - 16584. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Das, A. K. Gupta, P. W. Sims, C. A. Gelfand, J. E. Jentoft, and A. K. Banerjee Role of Cellular Casein Kinase II in the Function of the Phosphoprotein (P) Subunit of RNA Polymerase of Vesicular Stomatitis Virus J. Biol. Chem., October 13, 1995; 270(41): 24100 - 24107. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
