scholarly journals Characterization of Monoclonal Antibodies Raised against Recombinant Respiratory Syncytial Virus Nucleocapsid (N) Protein: Identification of a Region in the Carboxy Terminus of N Involved in the Interaction with P Protein

Virology ◽  
2001 ◽  
Vol 289 (2) ◽  
pp. 252-261 ◽  
Author(s):  
Jillian Murray ◽  
Colin Loney ◽  
Lindsay B. Murphy ◽  
Susan Graham ◽  
Robert P. Yeo
Keyword(s):  
Monoclonal Antibodies ◽  
Respiratory Syncytial Virus ◽  
Protein Identification ◽  
Carboxy Terminus ◽  
N Protein ◽  
P Protein ◽  
Syncytial Virus

Immunological Characterization of Respiratory Syncytial Virus N Protein Epitopes Recognized by Human Cytotoxic T Lymphocytes

2007 ◽  
Vol 20 (3) ◽  
pp. 399-406 ◽  
Author(s):  
Chiara Terrosi ◽  
Giuseppa Di Genova ◽  
Gianni Gori Savellini ◽  
Pierpaolo Correale ◽  
Patrizia Blardi ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
T Lymphocytes ◽  
Cytotoxic T Lymphocytes ◽  
Immunological Characterization ◽  
N Protein ◽  
Syncytial Virus

scholarly journals The Major Phosphorylation Sites of the Respiratory Syncytial Virus Phosphoprotein Are Dispensable for Virus Replication In Vitro

2002 ◽  
Vol 76 (21) ◽  
pp. 10776-10784 ◽  
Author(s):  
Bin Lu ◽  
Chien-Hui Ma ◽  
Robert Brazas ◽  
Hong Jin
Keyword(s):  
Respiratory Syncytial Virus ◽  
Virus Replication ◽  
Vero Cells ◽  
Phosphorylation Sites ◽  
N Protein ◽  
P Protein ◽  
Infected Cells ◽  
Syncytial Virus

ABSTRACT The phosphoprotein (P protein) of respiratory syncytial virus (RSV) is a key component of the viral RNA-dependent RNA polymerase complex. The protein is constitutively phosphorylated at the two clusters of serine residues (116, 117, and 119 [116/117/119] and 232 and 237 [232/237]). To examine the role of phosphorylation of the RSV P protein in virus replication, these five serine residues were altered to eliminate their phosphorylation potential, and the mutant proteins were analyzed for their functions with a minigenome assay. The reporter gene expression was reduced by 20% when all five phosphorylation sites were eliminated. Mutants with knockout mutations at two phosphorylation sites (S232A/S237A [PP2]) and at five phosphorylation sites (S116L/S117R/S119L/S232A/S237A [PP5]) were introduced into the infectious RSV A2 strain. Immunoprecipitation of 33Pi-labeled infected cells showed that P protein phosphorylation was reduced by 80% for rA2-PP2 and 95% for rA2-PP5. The interaction between the nucleocapsid (N) protein and P protein was reduced in rA2-PP2- and rA2-PP5-infected cells by 30 and 60%, respectively. Although the two recombinant viruses replicated well in Vero cells, rA2-PP2 and, to a greater extent, rA2-PP5, replicated poorly in HEp-2 cells. Virus budding from the infected HEp-2 cells was affected by dephosphorylation of P protein, because the majority of rA2-PP5 remained cell associated. In addition, rA2-PP5 was also more attenuated than rA2-PP2 in replication in the respiratory tracts of mice and cotton rats. Thus, our data suggest that although the major phosphorylation sites of RSV P protein are dispensable for virus replication in vitro, phosphorylation of P protein is required for efficient virus replication in vitro and in vivo.

scholarly journals Production and Characterization of Bovine Monoclonal Antibodies to Respiratory Syncytial Virus

1988 ◽  
Vol 69 (12) ◽  
pp. 3023-3032 ◽  
Author(s):  
H. E. Kennedy ◽  
B. V. Jones ◽  
E. M. Tucker ◽  
N. J. Ford ◽  
S. W. Clarke ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Respiratory Syncytial Virus ◽  
Syncytial Virus

Antigenic Characterization of Respiratory Syncytial Virus Strains with Monoclonal Antibodies

1985 ◽  
Vol 151 (4) ◽  
pp. 626-633 ◽  
Author(s):  
L. J. Anderson ◽  
J. C. Hierholzer ◽  
C. Tsou ◽  
R. M. Hendry ◽  
B. F. Fernie ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Respiratory Syncytial Virus ◽  
Antigenic Characterization ◽  
Syncytial Virus ◽  
Virus Strains
Sign in / Sign up

Export Citation Format

Share Document