Ebola virus Glycoprotein/GP-RBD Protein (ACI28624, HEK293, Fc)

Ebola virus glycoprotein (GP1), as a receptor-binding subunit, plays a key role in the virus entry process. During late stages of infection, GP1 downregulates key host cell surface molecules, including integrins such as ITGA1-6, disrupting adhesion and potentially leading to disruption of vascular integrity. Ebola virus Glycoprotein/GP-RBD Protein (ACI28624, HEK293, Fc) is the recombinant Virus-derived Ebola virus Glycoprotein/GP protein RBD, expressed by HEK293 , with C-hFc labeled tag.

The trimeric GP1,2 complexes of the Ebola virus Glycoprotein (GP) play a pivotal role in viral entry processes, where GP1 serves as the receptor-binding subunit and GP2 acts as the membrane fusion subunit. In the later stages of infection, GP1 down-regulates the expression of crucial host cell surface molecules involved in immune surveillance and cell adhesion. This includes the modulation of integrins such as ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV, and ITGB1, potentially leading to cell detachment and contributing to the disruption of blood vessel integrity, resulting in hemorrhages during infection (cytotoxicity). Additionally, GP1 interacts with host TLR4, stimulating the differentiation and activation of monocytes, leading to bystander death of T-lymphocytes. It further down-regulates the function of host natural killer cells and counteracts the antiviral effect of host BST2/tetherin, which restricts the release of progeny virions from infected cells. Interestingly, GP1 cooperates with VP40 and host BST2 to activate the canonical NF-kappa-B pathway in a manner dependent on neddylation. Furthermore, GP1 functions as a decoy for anti-GP1,2 antibodies, contributing to viral immune evasion, and interacts with host macrophages and dendritic cells, inducing the up-regulation of cytokine transcription, with this effect mediated through the activation of host TLR4.

Virus

HEK293

C-hFc

ACI28624.1 (I33-V308)

9487265  [NCBI]

Approximately 57.6 kDa.

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.