Structural insights into the Langya virus attachment glycoprotein

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Structure Pub Date : 2024-05-29 DOI:10.1016/j.str.2024.05.003

Chenghai Wang, Min Li, Yufan Wang, Qiang Ding, Shilong Fan, Jun Lan

引用次数: 0

Abstract

Langya virus (LayV) was recently detected in patients with acute pneumonic diseases in China. Genome alignment indicated that LayV is a type of zoonotic henipavirus (HNV) that might also infect domestic animals. Previous studies revealed that HNVs mainly use ephrin-B1, ephrin-B2, or ephrin-B3 as cell receptors and the attachment glycoprotein (G) is the host cell receptor-binding protein. However, the LayV receptor remains unknown. Here, we present the 2.77 Å crystal structure of the LayV G C-terminal domain (CTD). We show that the LayV G protein CTD possesses a similar architecture as the Mojiang virus (MojV) G protein but is markedly different from the Nipah virus (NiV), Hendra virus (HeV), and Cedar virus (CedV) G proteins. Surface plasmon resonance (SPR) experiments indicate that LayV G does not bind ephrin-B proteins. Steric hindrance may prevent interactions between LayV G and ephrin-B. Our data might facilitate drug development targeting LayV.

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对琅琊病毒附着糖蛋白结构的深入研究

中国最近在急性肺炎患者中发现了琅琊病毒（LayV）。基因组比对表明，琅琊病毒是一种人畜共患的鸡病毒（HNV），也可能感染家畜。以往的研究表明，HNV主要以ephrin-B1、ephrin-B2或ephrin-B3作为细胞受体，附着糖蛋白（G）是宿主细胞受体结合蛋白。然而，LayV受体仍然未知。在这里，我们展示了 LayV G C 端结构域（CTD）的 2.77 Å 晶体结构。我们发现，LayV G 蛋白 CTD 具有与墨江病毒 (MojV) G 蛋白相似的结构，但与尼帕病毒 (NiV)、亨德拉病毒 (HeV) 和雪松病毒 (CedV) G 蛋白有明显不同。表面等离子体共振（SPR）实验表明，LayV G 不会与 ephrin-B 蛋白结合。立体阻碍可能阻止了 LayV G 与 ephrin-B 之间的相互作用。我们的数据可能有助于开发针对 LayV 的药物。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Structure 生物-生化与分子生物学

CiteScore

8.90

自引率

1.80%

发文量

155

审稿时长

3-8 weeks

期刊介绍： Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome. In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.