| A Glycoprotein Mutation That Emerged during the 2013-2016 Ebola Virus Epidemic Alters Proteolysis and Accelerates Membrane Fusion. | A Glycoprotein Mutation That Emerged during the 2013-2016 Ebola Virus Epidemic Alters Proteolysis and Accelerates Membrane Fusion.
Fels JM, Bortz RH 3rd, Alkutkar T, Mittler E, Jangra RK, Spence JS, Chandran K., Free PMC Article | 11/13/2021 |
| A Virion-Based Assay for Glycoprotein Thermostability Reveals Key Determinants of Filovirus Entry and Its Inhibition. | A Virion-Based Assay for Glycoprotein Thermostability Reveals Key Determinants of Filovirus Entry and Its Inhibition.
Bortz RH 3rd, Wong AC, Grodus MG, Recht HS, Pulanco MC, Lasso G, Anthony SJ, Mittler E, Jangra RK, Chandran K., Free PMC Article | 11/28/2020 |
| The EBOV glycoprotein (GP1,2) is the sole viral envelope protein and a major component of immunogenicity; it is encoded by the GP gene along with two truncated versions: soluble GP (sGP) and small soluble GP (ssGP). sGP may subvert the host immune response by inducing antibodies against sGP rather than GP1,2. | The Roles of Ebola Virus Soluble Glycoprotein in Replication, Pathogenesis, and Countermeasure Development.
Zhu W, Banadyga L, Emeterio K, Wong G, Qiu X., Free PMC Article | 07/4/2020 |
| Growth-Adaptive Mutations in the Ebola Virus Makona Glycoprotein Alter Different Steps in the Virus Entry Pathway. | Growth-Adaptive Mutations in the Ebola Virus Makona Glycoprotein Alter Different Steps in the Virus Entry Pathway.
Ruedas JB, Arnold CE, Palacios G, Connor JH., Free PMC Article | 09/22/2018 |
| 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. | Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity.
Lee J, Nyenhuis DA, Nelson EA, Cafiso DS, White JM, Tamm LK., Free PMC Article | 06/9/2018 |
| Ebola virus GP directly subverts the host's immune response by increasing the susceptibility of monocytes to Ebola virus infection. | Ebola virus glycoprotein directly triggers T lymphocyte death despite of the lack of infection.
Iampietro M, Younan P, Nishida A, Dutta M, Lubaki NM, Santos RI, Koup RA, Katze MG, Bukreyev A., Free PMC Article | 11/25/2017 |
| 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 | Spontaneous Mutation at Amino Acid 544 of the Ebola Virus Glycoprotein Potentiates Virus Entry and Selection in Tissue Culture.
Ruedas JB, Ladner JT, Ettinger CR, Gummuluru S, Palacios G, Connor JH., Free PMC Article | 09/2/2017 |
| although Asn(563) and Asn(618) are not required for EBOV GP expression, they synergistically regulate its maturation, which determines its functionality. | Mechanistic understanding of N-glycosylation in Ebola virus glycoprotein maturation and function.
Wang B, Wang Y, Frabutt DA, Zhang X, Yao X, Hu D, Zhang Z, Liu C, Zheng S, Xiang SH, Zheng YH., Free PMC Article | 06/3/2017 |
| 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. | Ebola Viral Glycoprotein Bound to Its Endosomal Receptor Niemann-Pick C1.
Wang H, Shi Y, Song J, Qi J, Lu G, Yan J, Gao GF., Free PMC Article | 06/4/2016 |
| Study presents the 3.6 A crystal structure of Marburg virus (strain Ravn) GP in complex with a cross-reactive antibody, MR78, from a human survivor, and a lower resolution structure of the antibody bound to Ebola virus(strain Zaire) GP. | Structural basis for Marburg virus neutralization by a cross-reactive human antibody.
Hashiguchi T, Fusco ML, Bornholdt ZA, Lee JE, Flyak AI, Matsuoka R, Kohda D, Yanagi Y, Hammel M, Crowe JE Jr, Saphire EO., Free PMC Article | 05/2/2015 |
| 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. | Less is more: Ebola virus surface glycoprotein expression levels regulate virus production and infectivity.
Mohan GS, Ye L, Li W, Monteiro A, Lin X, Sapkota B, Pollack BP, Compans RW, Yang C., Free PMC Article | 04/18/2015 |
| Mucin-like domain is located at the apex and the sides of each glycoprotein monomer. | Spatial localization of the Ebola virus glycoprotein mucin-like domain determined by cryo-electron tomography.
Tran EE, Simmons JA, Bartesaghi A, Shoemaker CJ, Nelson E, White JM, Subramaniam S., Free PMC Article | 01/24/2015 |
| The glycoprotein's internal fusion loop is critical for viral entry and fusion. | Ebolavirus entry requires a compact hydrophobic fist at the tip of the fusion loop.
Gregory SM, Larsson P, Nelson EA, Kasson PM, White JM, Tamm LK., Free PMC Article | 10/4/2014 |
| GP play multiple functions including virus attachment and entry, cell rounding and cytotoxicity and down-regulation of host surface proteins.[review] | [Research progress on ebola virus glycoprotein].
Ding GY, Wang ZY, Gao L, Jiang BF. | 07/20/2013 |
| 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 | A mutation in the Ebola virus envelope glycoprotein restricts viral entry in a host species- and cell-type-specific manner.
Martinez O, Ndungo E, Tantral L, Miller EH, Leung LW, Chandran K, Basler CF., Free PMC Article | 06/8/2013 |
| Neither EBV GP nor HIV-1 Vpu had any effect on tetherin's distribution within lipid raft domains. | Anti-tetherin activities of HIV-1 Vpu and Ebola virus glycoprotein do not involve removal of tetherin from lipid rafts.
Lopez LA, Yang SJ, Exline CM, Rengarajan S, Haworth KG, Cannon PM., Free PMC Article | 06/23/2012 |
| 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. | Ebola virus entry requires the host-programmed recognition of an intracellular receptor.
Miller EH, Obernosterer G, Raaben M, Herbert AS, Deffieu MS, Krishnan A, Ndungo E, Sandesara RG, Carette JE, Kuehne AI, Ruthel G, Pfeffer SR, Dye JM, Whelan SP, Brummelkamp TR, Chandran K., Free PMC Article | 06/16/2012 |
| Ebola virus GP forms a tandem beta-hairpin structure that binds deeply into a cleft in the antibody-combining site. | Structure of an antibody in complex with its mucin domain linear epitope that is protective against Ebola virus.
Olal D, Kuehne AI, Bale S, Halfmann P, Hashiguchi T, Fusco ML, Lee JE, King LB, Kawaoka Y, Dye JM Jr, Saphire EO., Free PMC Article | 04/7/2012 |
| Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for efficient entry into cell lines and macrophages independent of TMPRSS2 expression. | Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for efficient entry into cell lines and macrophages independent of TMPRSS2 expression.
Gnirss K, Kühl A, Karsten C, Glowacka I, Bertram S, Kaup F, Hofmann H, Pöhlmann S., Free PMC Article | 03/24/2012 |
| Cathepsin L cleavage potentiates the Ebola virus GP to undergo a fusion-relevant conformational change. | Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.
Brecher M, Schornberg KL, Delos SE, Fusco ML, Saphire EO, White JM., Free PMC Article | 02/18/2012 |
| R64 and K95 of GP1 are involved in receptor binding. | Characterization of the receptor-binding domain of Ebola glycoprotein in viral entry.
Wang J, Manicassamy B, Caffrey M, Rong L., Free PMC Article | 10/1/2011 |
| liposome fusion data and NMR structures for a complete (54-residue) disulfide-bonded internal fusion loop (Ebov FL) in a membrane mimetic | Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.
Gregory SM, Harada E, Liang B, Delos SE, White JM, Tamm LK., Free PMC Article | 09/10/2011 |
| Axl enhances entry of Zaire ebolavirus without direct interactions with the viral glycoprotein. | Tyrosine kinase receptor Axl enhances entry of Zaire ebolavirus without direct interactions with the viral glycoprotein.
Brindley MA, Hunt CL, Kondratowicz AS, Bowman J, Sinn PL, McCray PB Jr, Quinn K, Weller ML, Chiorini JA, Maury W., Free PMC Article | 08/6/2011 |
| 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. | A new Ebola virus nonstructural glycoprotein expressed through RNA editing.
Mehedi M, Falzarano D, Seebach J, Hu X, Carpenter MS, Schnittler HJ, Feldmann H., Free PMC Article | 07/16/2011 |
| These findings suggest that Ebola virus GP uses a novel mechanism to circumvent tetherin restriction. | Ebola virus glycoprotein counteracts BST-2/Tetherin restriction in a sequence-independent manner that does not require tetherin surface removal.
Lopez LA, Yang SJ, Hauser H, Exline CM, Haworth KG, Oldenburg J, Cannon PM., Free PMC Article | 08/16/2010 |