CHIKV E1
Escherichia Coli.
Protein is >90% pure as determined by SDS-PAGE.
Description
Recombinant Chikungunya E1 produced in E.coli having a molecular weight of 48kDa.
Product Specs
Chikungunya, a viral infection transmitted to humans through the bites of infected Aedes mosquitoes (A. albopictus and A. aegypti), is characterized by fever and joint pain. The virus can also infect animals such as monkeys, birds, cattle, and rodents. After an incubation period of 2-4 days, individuals typically develop a high fever lasting 2-7 days. Joint pain, a hallmark of the disease, can persist for weeks, months, or even years. While generally non-fatal, chikungunya has a mortality rate of approximately 1 in 1,000 cases. Since 2004, outbreaks have been reported in Asia, Europe, and the Americas. The chikungunya virus (CHIKV) possesses a single-stranded positive-sense RNA genome, approximately 11,800 nucleotides in length, encoding two open reading frames. Its nucleocapsid, composed of the genomic RNA and capsid protein, is enclosed within a host-derived lipid bilayer studded with viral envelope proteins. These proteins form 80 glycoprotein spikes, anchored to the envelope, that mediate viral attachment, entry, and budding. The structural polyprotein is translated from a subgenomic mRNA, while the five structural proteins (capsid, E3, E2, 6K, E1) are produced as a single polyprotein. The capsid protein encapsidates the viral RNA, while the envelope polyprotein precursor undergoes processing in the endoplasmic reticulum, resulting in the formation of E3, E2, and E1. These proteins assemble into hetero-trimeric spikes, with E2 and E1 playing crucial roles in receptor binding, pH-dependent endocytosis, and viral budding.
Recombinant Chikungunya E1 protein, with a molecular weight of 48kDa, produced in E.coli.
The product is supplied as a sterile solution, filtered for purity, and formulated in phosphate-buffered saline (PBS).
CHIKV E1 remains stable for up to one week when stored at 4°C. However, for long-term storage, it is recommended to store the protein below -18°C to preserve its integrity. Repeated freezing and thawing of the product should be avoided.
The purity of the CHIKV E1 protein is greater than 90%, as determined by SDS-PAGE analysis, a widely used technique for assessing protein purity.
Escherichia Coli.
PNTVGVPYKTLVNRPGYSPMVLEMELLSVTLEPTLSLDYITCEYKTVIPSPYVKCCGTAECKDKSLPDYSC
KVFTGVYPFMWGGAYCFCDTENTQLSEAHVEKSESCKTEFASAYRAHTASASAKLRVLYQGNNVTVSAY
ANGDHAVTVKDAKFIVGPMSSAWTPFDNKIVVYKGDVYNMDYPPFGAGRPGQFGDIQSRTPESEDVYAN
TQLVLQRPSAGTVHVPYSQAPSGFKYWLKERGASLQHTAPFGCQIATNPVRAMNCAVGNMPISIDIPDAAF
TRVVDAPSLTDMSCEVPACTHSSDFGGVAIIKYAASKKGKCAVHSMTNAVTIREAEIEVEGNSQLQISFSTAL
ASAEFRVQVCSTQVHCAAECHPPKDHIVNYPASHTTLGVQDISVTAMSWVQKITG
Purified by proprietary chromatographic technique.
Product Science Overview
Chikungunya virus (CHIKV) is an arthropod-borne virus (arbovirus) that belongs to the genus Alphavirus within the family Togaviridae . It is primarily transmitted to humans through the bites of infected Aedes mosquitoes, particularly Aedes aegypti and Aedes albopictus . CHIKV is responsible for causing Chikungunya fever, a disease characterized by sudden onset of fever, severe joint pain, muscle pain, headache, nausea, fatigue, and rash .
The E1 protein of CHIKV is a glycoprotein that plays a crucial role in the virus’s ability to infect host cells. It is involved in the mediation of viral membrane fusion during infection, which is a critical step for the release of the viral genome into the host cytoplasm for replication . The E1 protein is part of the viral envelope and works in conjunction with the E2 glycoprotein to facilitate the entry of the virus into host cells .
To study the E1 protein and its functions, researchers have developed recombinant versions of the protein. Recombinant E1 protein can be produced using various expression systems, including insect cells infected with recombinant baculoviruses . This approach allows for the high-level expression of the E1 protein, which can then be purified and used for further studies.
Research has shown that the recombinant E1 protein retains its functional properties, including its ability to mediate membrane fusion . Studies involving site-directed mutagenesis have identified key amino acid residues in the E1 protein that are critical for its fusion activity . For example, mutations at residues G91 and H230 have been found to significantly reduce or abolish the fusion activity of the E1 protein .
The recombinant E1 protein has several important applications in the study of CHIKV and the development of potential treatments and vaccines. It can be used to:
- Investigate the molecular mechanisms of CHIKV entry and fusion with host cells .
- Develop assays for screening antiviral compounds that target the E1 protein .
- Generate neutralizing antibodies that can be used for therapeutic purposes .
- Serve as a component in subunit vaccines aimed at preventing CHIKV infections .
