scholarly journals Serodiagnosis Using Recombinant Nipah Virus Nucleocapsid Protein Expressed in Escherichia coli

2006 ◽  
Vol 44 (9) ◽  
pp. 3134-3138 ◽  
Author(s):  
F. Yu ◽  
N. S. Khairullah ◽  
S. Inoue ◽  
V. Balasubramaniam ◽  
S. J. Berendam ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Nucleocapsid Protein ◽  
Nipah Virus

scholarly journals Mutagenesis of the nucleocapsid protein of Nipah virus involved in capsid assembly

2009 ◽  
Vol 90 (2) ◽  
pp. 392-397 ◽  
Author(s):  
Swee Tin Ong ◽  
Khatijah Yusoff ◽  
Chiew Ling Kho ◽  
Janna Ong Abdullah ◽  
Wen Siang Tan
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Newcastle Disease ◽  
Nucleocapsid Protein ◽  
Nipah Virus ◽  
Capsid Assembly ◽  
Amino Acid Residues ◽  
N Protein ◽  
Capsid Formation ◽  
Carboxy Terminal

The nucleocapsid protein of Nipah virus produced in Escherichia coli assembled into herringbone-like particles. The amino- and carboxy-termini of the N protein were shortened progressively to define the minimum contiguous sequence involved in capsid assembly. The first 29 aa residues of the N protein are dispensable for capsid formation. The 128 carboxy-terminal residues do not play a role in the assembly of the herringbone-like particles. A region with amino acid residues 30–32 plays a crucial role in the formation of the capsid particle. Deletion of any of the four conserved hydrophobic regions in the N protein impaired capsid formation. Replacement of the central conserved regions with the respective sequences from the Newcastle disease virus restored capsid formation.

scholarly journals C-Terminal DxD-Containing Sequences within Paramyxovirus Nucleocapsid Proteins Determine Matrix Protein Compatibility and Can Direct Foreign Proteins into Budding Particles

2016 ◽  
Vol 90 (7) ◽  
pp. 3650-3660 ◽  
Author(s):  
Greeshma Ray ◽  
Phuong Tieu Schmitt ◽  
Anthony P. Schmitt
Keyword(s):  
Nucleocapsid Protein ◽  
Matrix Protein ◽  
Nipah Virus ◽  
Mumps Virus ◽  
Foreign Protein ◽  
Efficient Production ◽  
Nucleocapsid Proteins ◽  
Virus Like Particles ◽  
Ribonucleoprotein Complexes ◽  
M Proteins

ABSTRACTParamyxovirus particles are formed by a budding process coordinated by viral matrix (M) proteins. M proteins coalesce at sites underlying infected cell membranes and induce other viral components, including viral glycoproteins and viral ribonucleoprotein complexes (vRNPs), to assemble at these locations from which particles bud. M proteins interact with the nucleocapsid (NP or N) components of vRNPs, and these interactions enable production of infectious, genome-containing virions. For the paramyxoviruses parainfluenza virus 5 (PIV5) and mumps virus, M-NP interaction also contributes to efficient production of virus-like particles (VLPs) in transfected cells. A DLD sequence near the C-terminal end of PIV5 NP protein was previously found to be necessary for M-NP interaction and efficient VLP production. Here, we demonstrate that 15-residue-long, DLD-containing sequences derived from either the PIV5 or Nipah virus nucleocapsid protein C-terminal ends are sufficient to direct packaging of a foreign protein,Renillaluciferase, into budding VLPs. Mumps virus NP protein harbors DWD in place of the DLD sequence found in PIV5 NP protein, and consequently, PIV5 NP protein is incompatible with mumps virus M protein. A single amino acid change converting DLD to DWD within PIV5 NP protein induced compatibility between these proteins and allowed efficient production of mumps VLPs. Our data suggest a model in which paramyxoviruses share an overall common strategy for directing M-NP interactions but with important variations contained within DLD-like sequences that play key roles in defining M/NP protein compatibilities.IMPORTANCEParamyxoviruses are responsible for a wide range of diseases that affect both humans and animals. Paramyxovirus pathogens include measles virus, mumps virus, human respiratory syncytial virus, and the zoonotic paramyxoviruses Nipah virus and Hendra virus. Infectivity of paramyxovirus particles depends on matrix-nucleocapsid protein interactions which enable efficient packaging of encapsidated viral RNA genomes into budding virions. In this study, we have defined regions near the C-terminal ends of paramyxovirus nucleocapsid proteins that are important for matrix protein interaction and that are sufficient to direct a foreign protein into budding particles. These results advance our basic understanding of paramyxovirus genome packaging interactions and also have implications for the potential use of virus-like particles as protein delivery tools.

Development and Evaluation of Recombinant Nucleocapsid Protein Based Diagnostic ELISA for Detection of Nipah Virus Infection in Pigs

2015 ◽  
Vol 37 (2) ◽  
pp. 154-166 ◽  
Author(s):  
Diwakar D. Kulkarni ◽  
Govindarajalu Venkatesh ◽  
Chakradhar Tosh ◽  
Priyanka Patel ◽  
Anita Mashoria ◽  
...  
Keyword(s):  
Virus Infection ◽  
Nucleocapsid Protein ◽  
Nipah Virus ◽  
Recombinant Nucleocapsid Protein

scholarly journals Purification and Characterization of the Sin Nombre Virus Nucleocapsid Protein Expressed in Escherichia coli

2002 ◽  
Vol 24 (1) ◽  
pp. 171
Author(s):  
Colleen B. Jonsson ◽  
Juan Gallegos ◽  
Phillip Fero ◽  
William Severson ◽  
Xiaolin Xu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Nucleocapsid Protein ◽  
Sin Nombre Virus ◽  
Purification And Characterization
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