EBOV EBOV-G / Glycoprotein (His Tag)

EBOV EBOV-G / Glycoprotein (His Tag)

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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). Binding to the macrophage specific lectin CLEC10A also seem to enhance virus infectivity. Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory. Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection. Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L presumably induces a conformational change of GP2, unmasking its fusion peptide and initiating membranes fusion.

Envelope glycoprotein

GP

Q05320

GP

Baculovirus-Insect Cells

A DNA sequence encoding the Zaire ebolavirus (strain Mayinga 1976) GP (AAC54887.1) (Met1-Gln650) was expressed with a polyhistidine tag at the C-terminus.

EBOV

The recombinant Zaire ebolavirus (strain Mayinga 1976) GP consists 629 amino acids and predicts a molecular mass of 69.3 kDa.

> 95% as determined by SDS-PAGE