3ve0

Crystal structure of Sudan Ebolavirus Glycoprotein (strain Boniface) bound to 16F6

spinqualitylabelsall models 3ve0, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ve0 is a 4 chain structure with sequence from Mus musculus and Sudan ebolavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MAN, NAG Related: 3s88, 3csy Gene: GP (Sudan ebolavirus) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed There are five antigenically distinct ebolaviruses that cause hemorrhagic fever in humans or non-human primates (Ebola virus, Sudan virus, Reston virus, Tai Forest virus, and Bundibugyo virus). The small handful of antibodies known to neutralize the ebolaviruses bind to the surface glycoprotein termed GP(1,2). Curiously, some antibodies against them are known to neutralize in vitro but not protect in vivo, whereas other antibodies are known to protect animal models in vivo, but not neutralize in vitro. A detailed understanding of what constitutes a neutralizing and/or protective antibody response is critical for development of novel therapeutic strategies. Here, we show that paradoxically, a lower affinity antibody with restricted access to its epitope confers better neutralization than a higher affinity antibody against a similar epitope, suggesting that either subtle differences in epitope, or different characteristics of the GP(1,2) molecules themselves, confer differential neutralization susceptibility. Here, we also report the crystal structure of trimeric, prefusion GP(1,2) from the original 1976 Boniface variant of Sudan virus complexed with 16F6, the first antibody known to neutralize Sudan virus, and compare the structure to that of Sudan virus, variant Gulu. We discuss new structural details of the GP(1)-GP(2) clamp, thermal motion of various regions in GP(1,2) across the two viruses visualized, details of differential interaction of the crystallized neutralizing antibodies, and their relevance for virus neutralization. Structural basis for differential neutralization of ebolaviruses.,Bale S, Dias JM, Fusco ML, Hashiguchi T, Wong AC, Liu T, Keuhne AI, Li S, Woods VL Jr, Chandran K, Dye JM, Saphire EO Viruses. 2012 Apr;4(4):447-70. Epub 2012 Apr 5. PMID:22590681 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody

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