Recombinant Zaire ebolavirus Pre-small/secreted glycoprotein (GP)

1. Growth-Adaptive Mutations in the Ebola Virus Makona Glycoprotein Alter Different Steps in the Virus Entry Pathway. PMID: 30021890
2. the structure of the membrane proximal external region (MPER) connected to the TM domain: i.e., the missing parts of the EBOV GP2 structure. The structure, solved by solution NMR and EPR spectroscopy in membrane-mimetic environments, consists of a helix-turn-helix architecture that is independent of pH. PMID: 28874543
3. Ebola virus GP directly subverts the host's immune response by increasing the susceptibility of monocytes to Ebola virus infection. PMID: 28542576
4. report provides experimental evidence that the spontaneous mutation T544I is a tissue culture adaptation in certain cell lines and that it may be unique for the species Zaire ebolavirus; the mutation led to a marked increase in virus growth kinetics and conferred a robust growth advantage over wild-type rVSV-MAK-GP on Vero E6 cells PMID: 28539437
5. although Asn(563) and Asn(618) are not required for EBOV GP expression, they synergistically regulate its maturation, which determines its functionality. PMID: 28196864
6. Study determined the crystal structure of the primed GP (GPcl) of Ebola virus bound to domain C of NPC1 (NPC1-C); NPC1-C utilizes two protruding loops to engage a hydrophobic cavity on head of GPcl. Upon enzymatic cleavage and NPC1-C binding, conformational change in the GPcl further affects the state of the internal fusion loop, triggering membrane fusion. PMID: 26771495
7. GP1,2 expression levels have a profound effect on factors that contribute to virus fitness and RNA editing may be an important mechanism employed by EBOV to regulate GP1,2 expression in order to optimize virus production and infectivity. PMID: 25392212
8. Mucin-like domain is located at the apex and the sides of each glycoprotein monomer. PMID: 25008940
9. The glycoprotein's internal fusion loop is critical for viral entry and fusion. PMID: 24696482
10. GP play multiple functions including virus attachment and entry, cell rounding and cytotoxicity and down-regulation of host surface proteins.[review] PMID: 23757858
11. findings demonstrate that a GP mutant, GP-F88A, defective for entry into a variety of human cell types, including antigen-presenting cells (APCs) can mediate viral entry into mouse CD11b( ) APCs; studies suggest an important role for NPC1 in the differential entry of GP-F88A into mouse versus human APCs PMID: 23302883
12. Purified human NPC1 binds only to a cleaved form of Ebola virus spike glycoprotein that is generated within cells during entry, and only viruses containing cleaved glycoprotein can utilize a receptor retargeted to the cell surface. PMID: 22395071
13. Ebola virus GP forms a tandem beta-hairpin structure that binds deeply into a cleft in the antibody-combining site. PMID: 22171276
14. Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for efficient entry into cell lines and macrophages independent of TMPRSS2 expression. PMID: 22222211
15. Cathepsin L cleavage potentiates the Ebola virus GP to undergo a fusion-relevant conformational change. PMID: 22031933
16. R64 and K95 of GP1 are involved in receptor binding. PMID: 21667336
17. liposome fusion data and NMR structures for a complete (54-residue) disulfide-bonded internal fusion loop (Ebov FL) in a membrane mimetic PMID: 21690393
18. Axl enhances entry of Zaire ebolavirus without direct interactions with the viral glycoprotein. PMID: 21529875
19. While ssGP appears to share similar structural properties with sGP, it does not appear to have the same anti-inflammatory function on endothelial cells as sGP. PMID: 21411529
20. These findings suggest that Ebola virus GP uses a novel mechanism to circumvent tetherin restriction. PMID: 20444895
21. CatB cleavage is required to facilitate the triggering of viral membrane fusion by destabilizing the prefusion conformation of EBOV GP PMID: 19846533
22. Ebola virus GP cytotoxicity is regulated by dynamin-dependent cellular protein trafficking PMID: 15596847
23. The transmembrane region of GP2 modifies the permeability of the plasma membrane. PMID: 16927113
24. the crystal structure of EBOV GP in its trimeric, pre-fusion conformation (GP1+GP2) bound to a neutralizing antibody, KZ52, derived from a human survivor of the 1995 Kikwit outbreak PMID: 18615077
25. The authors show that the mucin domain from the highly pathogenic Zaire subtype of Ebola virus is sufficient to cause characteristic cytopathology when expressed in the context of a foreign glycoprotein. PMID: 19013626

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