Ebolavirus (EBOV) is a negative-stranded, membrane-enveloped filovirus that causes a severe hemorrhagic fever in both humans and non-human primates. Since its discovery in central Africa in 1976, five species of EBOV have been isolated: Zaire (ZEBOV), Sudan, Côte d’Ivoire, Reston (REBOV) and the proposed ‘Bundibugyo’ EBOV. The EBOV genome contains seven genes: NP, VP35, VP40, GP, VP30, VP24 and L. However, more than seven proteins are produced owing to cotranscriptional editing and post-translational processing of the GP gene and gene products. The virion-attached glycoprotein (GP) is critical in the EBOV life cycle, as it is solely responsible for attachment, fusion and entry of target cells. Moreover, GP is responsible for critical pathogenic differences among viral species. However, the role of GP cytotoxicity in EBOV pathogenesis remains poorly defined, as constitutive expression of EBOV GP at moderate levels do not cause cell rounding and is not cytotoxic. Here you can see a recent crystal structure of the glycoprotein from Ebola Virus (EBOV) showing its rich glycosylation pattern (PDB code: 7JPI)
#molecularart ... #immolecular ... #ebola ... #virus ... #glycoprotein ... #infection ... #extracellular ... #xray
Structure of the Ebola virus glycoprotein rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #ebola ... #virus ... #glycoprotein ... #infection ... #extracellular ... #xray
Structure of the Ebola virus glycoprotein rendered with @proteinimaging and depicted with @corelphotopaint
