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8ILQ

Structure of SFTSV Gn-Gc heterodimer

Summary for 8ILQ
Entry DOI10.2210/pdb8ilq/pdb
EMDB information35540
DescriptorEnvelopment polyprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordssftsv, virion, icosahedral reconstruction, virus, viral protein
Biological sourceSevere fever with thrombocytopenia syndrome virus
More
Total number of polymer chains2
Total formula weight118055.28
Authors
Du, S.,Peng, R.,Qi, J.,Li, C. (deposition date: 2023-03-04, release date: 2023-09-13, Last modification date: 2024-03-27)
Primary citationDu, S.,Peng, R.,Xu, W.,Qu, X.,Wang, Y.,Wang, J.,Li, L.,Tian, M.,Guan, Y.,Wang, J.,Wang, G.,Li, H.,Deng, L.,Shi, X.,Ma, Y.,Liu, F.,Sun, M.,Wei, Z.,Jin, N.,Liu, W.,Qi, J.,Liu, Q.,Liao, M.,Li, C.
Cryo-EM structure of severe fever with thrombocytopenia syndrome virus.
Nat Commun, 14:6333-6333, 2023
Cited by
PubMed Abstract: The severe fever with thrombocytopenia syndrome virus (SFTSV) is a tick-borne human-infecting bunyavirus, which utilizes two envelope glycoproteins, Gn and Gc, to enter host cells. However, the structure and organization of these glycoproteins on virion surface are not yet known. Here we describe the structure of SFTSV determined by single particle reconstruction, which allows mechanistic insights into bunyavirus assembly at near-atomic resolution. The SFTSV Gn and Gc proteins exist as heterodimers and further assemble into pentameric and hexameric peplomers, shielding the Gc fusion loops by both intra- and inter-heterodimer interactions. Individual peplomers are associated mainly through the ectodomains, in which the highly conserved glycans on N914 of Gc play a crucial role. This elaborate assembly stabilizes Gc in the metastable prefusion conformation and creates some cryptic epitopes that are only accessible in the intermediate states during virus entry. These findings provide an important basis for developing vaccines and therapeutic drugs.
PubMed: 37816705
DOI: 10.1038/s41467-023-41804-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.3 Å)
Structure validation

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