6LGX

Structure of Rabies virus glycoprotein at basic pH

Summary for 6LGX

• Entry DOI: 10.2210/pdb6lgx/pdb
• Descriptor: Glycoprotein,Glycoprotein,Glycoprotein (1 entity in total)
• Functional Keywords: functional class, viral protein
• Biological source: Rabies lyssavirus; More
• Total number of polymer chains: 2
• Total formula weight: 99266.56

Authors

Yang, F.L.,Lin, S.,Ye, F.,Yang, J.,Qi, J.X.,Chen, Z.J.,Lin, X.,Wang, J.C.,Yue, D.,Cheng, Y.W.,Chen, Z.M.,Chen, H.,You, Y.,Zhang, Z.L.,Yang, Y.,Yang, M.,Sun, H.L.,Li, Y.H.,Cao, Y.,Yang, S.Y.,Wei, Y.Q.,Gao, G.F.,Lu, G.W. (deposition date: 2019-12-06, release date: 2020-02-19, Last modification date: 2024-10-09)

Primary citation

Yang, F.,Lin, S.,Ye, F.,Yang, J.,Qi, J.,Chen, Z.,Lin, X.,Wang, J.,Yue, D.,Cheng, Y.,Chen, Z.,Chen, H.,You, Y.,Zhang, Z.,Yang, Y.,Yang, M.,Sun, H.,Li, Y.,Cao, Y.,Yang, S.,Wei, Y.,Gao, G.F.,Lu, G.
Structural Analysis of Rabies Virus Glycoprotein Reveals pH-Dependent Conformational Changes and Interactions with a Neutralizing Antibody.
Cell Host Microbe, 27:441-, 2020

PubMed Abstract: Rabies virus (RABV), the etiological agent for the lethal disease of rabies, is a deadly zoonotic pathogen. The RABV glycoprotein (RABV-G) is a key factor mediating virus entry and the major target of neutralizing antibodies. Here, we report the crystal structures of RABV-G solved in the free form at ∼pH-8.0 and in the complex form with a neutralizing antibody 523-11 at ∼pH-6.5, respectively. RABV-G has three domains, and the basic-to-acidic pH change results in large domain re-orientations and concomitant domain-linker re-constructions, switching it from a bent hairpin conformation into an extended conformation. During such low-pH-induced structural transitions, residues located in the domain-linker are found to play important roles in glycoprotein-mediated membrane fusion. Finally, the antibody interacts with RABV-G mainly through its heavy chain and binds to a bipartite conformational epitope in the viral protein for neutralization. These structures provide valuable information for vaccine and drug design.

PubMed: 32004500
DOI: 10.1016/j.chom.2019.12.012

Experimental method

X-RAY DIFFRACTION (3.097 Å)