Lassa Capsid is >90% pure as determined by 10% PAGE (coomassie staining).
The E.Coli derived Recombinant Lassa Nucleoprotein (LASV strain AV, GenBank accession number AAG41803) containing 420 amino acids of Lassa virus nucleoprotein.
The Lassa Capsid protein is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic technique.
This recombinant Lassa Nucleoprotein is derived from E. coli and corresponds to the LASV strain AV (GenBank: AAG41803). It encompasses 420 amino acids of the Lassa virus nucleoprotein. The protein is engineered with a C-terminal 6xHis tag to facilitate purification via chromatography.
The Lassa Capsid protein is supplied in a solution containing 25mM Tris Base and 10mM K2CO3.
Analysis by 10% PAGE (coomassie staining) confirms that the Lassa Capsid protein is greater than 90% pure.
Lassa fever, caused by the Lassa virus (LASV), is a severe and often fatal hemorrhagic illness endemic to West Africa. The virus belongs to the Arenaviridae family and is responsible for an estimated 300,000 to 500,000 infections annually, with a mortality rate of 15% to 20% among hospitalized patients . Despite its significant impact on public health, there is currently no licensed vaccine or specific antiviral treatment available for Lassa fever .
The Lassa virus is an enveloped, single-stranded RNA virus. Its genome encodes four proteins: the nucleoprotein (NP), the glycoprotein precursor (GPC), the matrix protein (Z), and the RNA-dependent RNA polymerase (L). The nucleoprotein is crucial for viral replication and transcription, while the glycoprotein precursor is cleaved into two subunits, GP1 and GP2, which are essential for viral entry into host cells .
Recombinant Lassa virus proteins, including the capsid protein, have been developed to facilitate research and the development of diagnostic tools, vaccines, and therapeutic agents. These recombinant proteins are typically produced using bacterial-based expression systems, such as Escherichia coli (E. coli), which allow for the efficient production and purification of viral proteins .
The expression and purification of recombinant Lassa virus proteins involve several steps. First, the gene encoding the target protein is cloned into an expression vector, which is then introduced into E. coli cells. The bacterial cells are cultured, and the recombinant protein is expressed as a fusion protein with a tag, such as maltose-binding protein (MBP), to facilitate purification . The fusion protein is then purified using affinity chromatography, cleaved to remove the tag, and further purified using size-exclusion chromatography .
Recombinant Lassa virus proteins have several applications in research and public health. They can be used to develop diagnostic assays for the early detection of Lassa fever, which is crucial for the timely administration of antiviral treatments like ribavirin . Additionally, these proteins are valuable tools for studying the immune response to LASV infection and for developing vaccines that can elicit protective immunity .
Recent advances in vaccine development have focused on mRNA-based vaccines, which have shown promise in preclinical studies. For example, mRNA-lipid nanoparticle (mRNA-LNP)-based vaccines expressing the LASV glycoprotein precursor or nucleoprotein have been shown to induce protective immunity in mouse models . These findings provide a critical foundation for the rapid development of effective Lassa virus vaccines .