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Open data
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Basic information
| Entry | Database: PDB / ID: 9x3k | |||||||||||||||||||||||||||
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| Title | apo state of Mengla Virus Glycoprotein | |||||||||||||||||||||||||||
Components | Envelope glycoprotein | |||||||||||||||||||||||||||
Keywords | VIRAL PROTEIN / Mengla Virus Glycoprotein | |||||||||||||||||||||||||||
| Function / homology | TLV/ENV coat polyprotein / : / Filoviruses glycoprotein, extracellular domain / Filovirus glycoprotein / Envelope glycoprotein GP2-like, HR1-HR2 / viral envelope / host cell plasma membrane / Envelope glycoprotein Function and homology information | |||||||||||||||||||||||||||
| Biological species | Dianlovirus menglaense | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.08 Å | |||||||||||||||||||||||||||
Authors | Wang, L. / Zou, B. / Liu, B. / Xue, L. / He, J. / Xiong, X. | |||||||||||||||||||||||||||
| Funding support | China, 2items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2026Title: Cryo-EM structures of Měnglà virus GP reveal combined Ebola- and Marburg-like epitope masking strategies for antibody evasion. Authors: Longyu Wang / Binqian Zou / Banghui Liu / Yong Ma / Lu Xue / Gul Habib / Xinglou Yang / Xinwen Chen / Jiantao Chen / Jincun Zhao / Ying Zhang / Zifeng Yang / Jun He / Xiaoli Xiong / ![]() 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 ...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. | |||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9x3k.cif.gz | 195.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9x3k.ent.gz | 148.2 KB | Display | PDB format |
| PDBx/mmJSON format | 9x3k.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x3/9x3k ftp://data.pdbj.org/pub/pdb/validation_reports/x3/9x3k | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 66502MC ![]() 9x3jC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
| #1: Protein | Mass: 73748.773 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Dianlovirus menglaense / Gene: GP / Production host: Homo sapiens (human) / References: UniProt: A0A3S8UVK3#2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Sugar | Has ligand of interest | N | Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: glycoprotein of mengla virus / Type: COMPLEX / Entity ID: #1 / Source: NATURAL |
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| Source (natural) | Organism: Dianlovirus menglaense |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Details of virus | Empty: YES / Enveloped: YES / Isolate: SUBSPECIES / Type: VIROID |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2400 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Symmetry | Point symmetry: C3 (3 fold cyclic) | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.08 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19463 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.08 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Dianlovirus menglaense
China, 2items
Citation


PDBj


Homo sapiens (human)

FIELD EMISSION GUN