9X3J
Glycoprotein of Mengla Virus with MR191 Fab bound
Summary for 9X3J
| Entry DOI | 10.2210/pdb9x3j/pdb |
| EMDB information | 66501 |
| Descriptor | Envelope glycoprotein, MR191 Fab Heavy Chain, MR191 Fab Light Chain, ... (6 entities in total) |
| Functional Keywords | mengla virus glycoprotein, viral protein |
| Biological source | Dianlovirus menglaense More |
| Total number of polymer chains | 9 |
| Total formula weight | 369042.41 |
| Authors | |
| Primary citation | Wang, L.,Zou, B.,Liu, B.,Ma, Y.,Xue, L.,Habib, G.,Yang, X.,Chen, X.,Chen, J.,Zhao, J.,Zhang, Y.,Yang, Z.,He, J.,Xiong, X. Cryo-EM structures of Mengla virus GP reveal combined Ebola- and Marburg-like epitope masking strategies for antibody evasion. Proc.Natl.Acad.Sci.USA, 123:e2529436123-e2529436123, 2026 Cited by PubMed Abstract: Ebola virus (EBOV) and Marburg virus (MARV) are highly lethal filoviruses that cause severe hemorrhagic fever in humans. A recently identified bat-borne filovirus, Měnglà virus (MLAV), uses the same NPC1 receptor as EBOV and MARV, raising concerns about its potential cross-species transmission. Here, we report cryo-EM structures of the MLAV surface glycoprotein (GP) in its unbound form and in complex with the MARV-neutralizing antibody MR191. MLAV GP exhibits distinctive structural features in the Wing and heptad repeat 1D (HR1D) regions, retains a visible Cap structure even after protease treatment, and contains a MARV GP-like α2 helix. MR191, a broadly neutralizing marburgvirus antibody that targets the conserved NPC1 receptor-binding pocket in MLAV GP, nonetheless exhibits impaired neutralizing activity, likely due to shielding by the MLAV Cap. In addition, the MLAV mucin-like domain, α2 helix, and HR1A region hinder binding by representative broadly neutralizing ebolavirus antibodies targeting the GP-waist, including 6D6, CA45, ADI-15878, and ADI-15946. Together, these results provide the first structural insights into MLAV GP and identify immune evasion driven by structural and sequence divergence as a major challenge for pan-filovirus antibody development. PubMed: 42247561DOI: 10.1073/pnas.2529436123 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.47 Å) |
Structure validation
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