Rabbit Polyclonal VGP antibody - conjugated to Biotin. Carrier free. Suitable for WB and reacts with Marburg virus samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Lake Victoria marburgvirus - Angola2005 GP aa 400 to C-terminus.
Constituents: 100% PBS
| WB | |
|---|---|
| Marburg virus | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Marburg virus | Dilution info Use at an assay dependent concentration. | Notes - |
GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection) (By similarity). GP2 acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide (By similarity).
Envelope glycoprotein, Virion spike glycoprotein, GP
Rabbit Polyclonal VGP antibody - conjugated to Biotin. Carrier free. Suitable for WB and reacts with Marburg virus samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Lake Victoria marburgvirus - Angola2005 GP aa 400 to C-terminus.
Constituents: 100% PBS
The purified antibody was conjugated with biotin at a molar ratio of 20:1 (Biotin: antibody), and purified from unconjugated biotin by diafiltration.
The MARV GP also known as Marburg virus glycoprotein is a critical protein in the structure of the Marburg virus. This glycoprotein plays a central role in viral entry into host cells by mediating attachment and fusion. MARV GP has a mass of approximately 9 kilodaltons and is expressed on the surface of the Marburg virus. The protein's function is essential for the virus to enter human cells facilitating its ability to spread and multiply in the host.
The Marburg virus glycoprotein aids the virus in evading host immune responses. It is part of a complex that involves other viral proteins enhancing its role in the viral lifecycle. MARV GP helps the virus adhere to host cell membranes subsequently triggering endocytosis—a process where the cell membrane engulfs the virus. This capability allows the virus to replicate inside the host efficiently and complicates the ability of the immune system to detect and eliminate the virus.
MARV GP interaction is important within the fusion and endocytosis pathways. It operates alongside cellular proteins that facilitate endocytic uptake such as clathrin and dynamin. MARV GP binding triggers a cascade that utilizes several host cell pathways to ensure fusion of the viral envelope with the host cell membrane enabling the entry of viral RNA into the host cytoplasm. This cooperative action permits seamless integration into the host cell processes.
MARV GP is directly implicated in the pathogenicity of Marburg virus disease a severe and fatal hemorrhagic fever. It shares similarities with proteins in Ebola virus such as Ebola virus glycoprotein which contributes to similar symptoms. Both glycoproteins introduce challenges in developing effective vaccines and therapeutics as they are involved in virus escape from immune detection. Understanding the role of MARV GP in disease mechanisms can drive better-targeted treatments and interventions.
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