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West Nile Virus Pre-Membrane (prM) Protein

$447.95$1,680.20 excl. VAT

West Nile virus pre-Membrane (prM) protein is a recombinant antigen, cloned and expressed in E. coli with greater than 95% purity. Antigen contains the West Nile virus N-terminal pre-Membrane (prM) immunodominant regions (aa 117-252) fused to a His-tag, for use in ELISA and other immunoassays.

WEST NILE VIRUS PRE-MEMBRANE (prM) PROTEIN

West Nile virus pre-Membrane (prM) protein is a recombinant antigen, cloned and expressed in E. coli with greater than 95% purity.

 

PRODUCT DETAILS – WEST NILE VIRUS PRE-MEMBRANE

  • West Nile virus pre-Membrane (prM) protein.
  • Recombinant 20 kDa protein manufactured in E. coli, with a 6xHis tag.
  • Contains N-terminal pre-Membrane (prM) immunodominant regions (aa 117-252).
  • Purity >95% as determined by SDS-PAGE.
  • For use in ELISA and other immunoassays.

 

BACKGROUND

West Nile virus (WNV) is an emerging mosquito-borne virus of the family Flaviviridae which is maintained in nature in an enzootic transmission cycle between avian hosts and mosquito vectors (Martín-Acebes and Saiz, 2012). WNV causes a broad spectrum of disease severity, ranging from fever to encephalitis and flaccid paralysis in both animals and humans. Most human infections with WNV (~80%) are asymptomatic, and symptomatic infections may vary from flu-like malaise to serious neuroinvasive diseases. Since its discovery in 1937, West Nile virus has spread to every continent except Antarctica. It is now the most widespread cause of arboviral neurological disease in the world, with no vaccine available and limited treatment options (reviewed in Chancey et al., 2015).

WNV is a small enveloped virus (~50 nm diameter) with an 11 kbp genome of positive-stranded RNA that is translated into a viral polyprotein and processed by viral and cellular enzymes to form three structural proteins [capsid (C), premembrane/membrane (prM/M) and envelope (E)] and seven nonstructural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B and NS5) (reviewed in Heinz and Stiasny, 2012). During viral assembly, E and prM associate to produce heterodimers before interaction with the nucleocapsid complex and forming immature virus. The prM proteins are cleaved by host furin protease into M proteins to release the mature virions through exocytosis (Lindenbach and Rice, 2001; Brinton, 2002). prM is thought to protect the immature virion from undergoing premature fusion prior to viral budding from the cell surface by blocking the fusion loop of E and is cleaved off during the viral maturation process (reviewed in Chancey et al., 2015).

This recombinant protein has been developed to help meet the need for improved research and surveillance diagnostics and the future development of vaccine candidates.

 

REFERENCES

  • Brinton MA (2002) The molecular biology of West Nile Virus: a new invader of the western hemisphere. Annu Rev Microbiol 56: 371–402.
  • Chancey et al. (2015). The Global Ecology and Epidemiology of West Nile Virus. BioMed Research International. Volume 2015, Article ID 376230, 20 pages.
  • Heinz F. X. and Stiasny,K. (2012). Flaviviruses and their antigenic structure, Journal of Clinical Virology, vol. 55, no. 4, pp. 289–295.
  • Lindenbach and Rice (2001) Flaviviridae: The viruses and their replication. In: Knipe DM, Howley PM, editors. Fields Virology. Philadelphia: Lippincott Williams & Wilkins. pp. 991–1041.
  • Martín-Acebes and Saiz (2012). West Nile virus: A re-emerging pathogen revisited. World J Virol. 1(2): 51-70.

 

Certificate of analysis
Safety datasheet

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