MEASLES VIRUS LARGE POLYMERASE RECOMBINANT PROTEIN
Measles virus Large Polymerase recombinant protein antigen is manufactured in E. coli with greater than 95% purity.
- Measles virus Large Polymerase recombinant protein
- Recombinant protein produced in E. coli. Comprises the large polymerase immunodominant regions, 58-149 amino acids.
- >95% purity as determined by 10% PAGE (Coomassie staining) and RP-HPLC.
- Presented in 50mM Tris-HCl, pH 8.0, 60mM NaCl, 10mM glutathione, 0.1% sarcosyl and 50% glycerol.
- Can be used as antigen in ELISA and Western Blots. Immunoreactive with sera of Measles virus infected individuals.
Measles virus (MV) is the type species of the Morbillivirus genus, which is one of the seven genera of the family Paramyxoviridae. It is a highly contagious, re-emerging, major human pathogen. It is a globally widespread disease that affects children but can also cause disease in unvaccinated adults. Humans are the only known host of measles virus and infection is spread from person-to-person via respiratory aerosol droplets, nasal secretions or through direct contact with infected individuals.
MVs are enveloped and contain single-stranded, negative-sense RNA genomes of 9-19 kbp. The MV single-stranded RNA genome is enclosed by nucleocapsid (N) proteins into helical ribonucleoprotein (RNP) complexes comprising of nucleo- (N), phospho- (P), and large (L) proteins. Encapsidated RNAs act as templates for transcription and replication by the viral RNA-dependent RNA-polymerases (RdRPs) complexes (Gutsche et al., 2015). Unencapsidated viral genomic RNA is transcriptionally inactive and not infectious (Duprex et al., 2002).
MeV has an RNA-dependent RNA polymerase composed of two viral polypeptides, a large protein, L, and a phosphoprotein, P, for transcription and replication of their genome. The L protein confers the RNA polymerase activity on the complex while the P protein acts as a transcription factor. Replication requires a viral RNA-dependent RNA polymerase (RdRP) consisting of the large (L) polymerase protein complexed with the homo-tetrameric phosphoprotein (P) (Du Pont et al., 2019).
- Du Pont et al. (2019). Bipartite interface of the measles virus phosphoprotein X domain with the large polymerase protein regulates viral polymerase dynamics. PLoS Pathog 15(8): e1007995.
- Duprex et al. (2002). Modulating the Function of the Measles Virus RNA-Dependent RNA Polymerase by Insertion of Green Fluorescent Protein into the Open Reading Frame. J Virol. 76(14): 7322–7328.
- Gutsche et al. (2015). Near-atomic cryo-EM structure of the helical measles virus nucleocapsid. Science. 348(6235):704–7.