6CV0

Cryo-electron microscopy structure of infectious bronchitis coronavirus spike protein

Summary for 6CV0

• Entry DOI: 10.2210/pdb6cv0/pdb
• EMDB information: 7631
• Related PRD ID: PRD_900017
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: infectious bronchitis coronavirus, spike, pre-fusion, cryo-em, viral protein
• Biological source: Infectious bronchitis virus
• Total number of polymer chains: 3
• Total formula weight: 384631.80

Authors

Shang, J.,Zheng, Y.,Yang, Y.,Liu, C.,Geng, Q.,Luo, C.,Zhang, W.,Li, F. (deposition date: 2018-03-27, release date: 2018-04-18, Last modification date: 2024-11-06)

Primary citation

Shang, J.,Zheng, Y.,Yang, Y.,Liu, C.,Geng, Q.,Luo, C.,Zhang, W.,Li, F.
Cryo-EM structure of infectious bronchitis coronavirus spike protein reveals structural and functional evolution of coronavirus spike proteins.
PLoS Pathog., 14:e1007009-e1007009, 2018

PubMed Abstract: As cell-invading molecular machinery, coronavirus spike proteins pose an evolutionary conundrum due to their high divergence. In this study, we determined the cryo-EM structure of avian infectious bronchitis coronavirus (IBV) spike protein from the γ-genus. The trimeric IBV spike ectodomain contains three receptor-binding S1 heads and a trimeric membrane-fusion S2 stalk. While IBV S2 is structurally similar to those from the other genera, IBV S1 possesses structural features that are unique to different other genera, thereby bridging these diverse spikes into an evolutionary spectrum. Specifically, among different genera, the two domains of S1, the N-terminal domain (S1-NTD) and C-terminal domain (S1-CTD), diverge from simpler tertiary structures and quaternary packing to more complex ones, leading to different functions of the spikes in receptor usage and membrane fusion. Based on the above structural and functional comparisons, we propose that the evolutionary spectrum of coronavirus spikes follows the order of α-, δ-, γ-, and β-genus. This study has provided insight into the evolutionary relationships among coronavirus spikes and deepened our understanding of their structural and functional diversity.

PubMed: 29684066
DOI: 10.1371/journal.ppat.1007009

Experimental method

ELECTRON MICROSCOPY (3.93 Å)