• <menu id="skkke"><tt id="skkke"></tt></menu>
  • <nav id="skkke"></nav>
  • 當前位置:  首頁 >> 最新重要論文

    最新重要論文

    Structure of Venezuelan equine encephalitis virus with its receptor LDLRAD3, Nature, 13 Oct 2021

    發布時間:2021年10月13日

    Nature, 13 October, 2021, DOI:https://doi.org/10.1038/s41586-021-03909-1

    Structure of Venezuelan equine encephalitis virus with its receptor LDLRAD3

    Bingting Ma, Cuiqing Huang, Jun Ma, Ye Xiang & Xinzheng Zhang 

    Abstract

    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.

    文章鏈接:https://www.nature.com/articles/s41586-021-03909-1

    相關報道:http://www.kevinscanvas.com/kyjz/zxdt/202110/t20211011_6220868.html

     

     

        附件下載:
    日本人成在线播放免费课体台
  • <menu id="skkke"><tt id="skkke"></tt></menu>
  • <nav id="skkke"></nav>