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-Structure paper
タイトル | Structure of Venezuelan equine encephalitis virus with its receptor LDLRAD3. |
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ジャーナル・号・ページ | Nature, Vol. 598, Issue 7882, Page 677-681, Year 2021 |
掲載日 | 2021年10月13日 |
著者 | Bingting Ma / Cuiqing Huang / Jun Ma / Ye Xiang / Xinzheng Zhang / |
PubMed 要旨 | Venezuelan equine encephalitis virus (VEEV) is an enveloped RNA virus that causes encephalitis and potentially mortality in infected humans and equines. At present, no vaccines or drugs are available ...Venezuelan equine encephalitis virus (VEEV) is an enveloped RNA virus that causes encephalitis and potentially mortality in infected humans and equines. At present, no vaccines or drugs are available that prevent or cure diseases caused by VEEV. Low-density lipoprotein receptor class A domain-containing 3 (LDLRAD3) was recently identified as a receptor for the entry of VEEV into host cells. Here we present the cryo-electron microscopy structure of the LDLRAD3 extracellular domain 1 (LDLRAD3-D1) in complex with VEEV virus-like particles at a resolution of 3.0 Å. LDLRAD3-D1 has a cork-like structure and is inserted into clefts formed between adjacent VEEV E2-E1 heterodimers in the viral-surface trimer spikes through hydrophobic and polar contacts. Mutagenesis studies of LDLRAD3-D1 identified residues that are involved in the key interactions with VEEV. Of note, some of the LDLRAD3-D1 mutants showed a significantly increased binding affinity for VEEV, suggesting that LDLRAD3-D1 may serve as a potential scaffold for the development of inhibitors of VEEV entry. Our structures provide insights into alphavirus assembly and the binding of receptors to alphaviruses, which may guide the development of therapeutic countermeasures against alphaviruses. |
リンク | Nature / PubMed:34646021 |
手法 | EM (単粒子) |
解像度 | 3.0 - 3.5 Å |
構造データ | EMDB-31566, PDB-7ffe: EMDB-31567, PDB-7fff: EMDB-31568, PDB-7ffl: EMDB-31569, PDB-7ffn: EMDB-31570, PDB-7ffo: EMDB-31571, PDB-7ffq: |
化合物 | ChemComp-CA: |
由来 |
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キーワード | VIRUS LIKE PARTICLE / Virus / Receptor / Complex / VIRUS LIKE PARTICLE/PROTEIN BINDING / VIRUS LIKE PARTICLE-PROTEIN BINDING complex |