Scholarlink

<p>Both autophagy and heat shock proteins (HSPs) play dual roles in viral infections, yet their coordination in antiviral defense remains unclear. Here, we show that a cytosolic small heat shock protein (AcsHSP) and a type II J-domain protein (AcDNAJB13) from areca palm interact with the coat protein (CP) of <i>areca palm velarivirus 1</i> (APV1) independently of HSP70 chaperones. Their closest <i>Nicotiana benthamiana</i> homologs also bind CP. Both APV1 infection and CP expression induces the transcription of <i>sHSP</i> and <i>DNAJB13</i>, which in turn inhibits CP accumulation. Silencing of these genes enhances APV1 infection and CP accumulation, while overexpression of <i>AcsHSP</i> reduces viral accumulation. Mechanistically, CP is degraded via autophagy. Both AcsHSP and AcDNAJB13 interact with the autophagosome marker ATG8f1. However, AcsHSP strengthens CP-ATG8f1 binding, whereas AcDNAJB13 weakens it. These findings reveal distinct yet complementary mechanisms by which sHSP and DNAJB13 coordinate with autophagy to restrict viral infection.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Small heat shock and J-domain proteins direct defense against areca palm velarivirus 1 by degrading coat protein via autophagy

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年4月28日

查看全文
  • Ruibai Zhao,
  • Jie Lu,
  • Zengyu Xing,
  • Jinling Zhai,
  • Hongxing Wang,
  • Xianmei Cao,
  • Xi Huang

摘要

Both autophagy and heat shock proteins (HSPs) play dual roles in viral infections, yet their coordination in antiviral defense remains unclear. Here, we show that a cytosolic small heat shock protein (AcsHSP) and a type II J-domain protein (AcDNAJB13) from areca palm interact with the coat protein (CP) of areca palm velarivirus 1 (APV1) independently of HSP70 chaperones. Their closest Nicotiana benthamiana homologs also bind CP. Both APV1 infection and CP expression induces the transcription of sHSP and DNAJB13, which in turn inhibits CP accumulation. Silencing of these genes enhances APV1 infection and CP accumulation, while overexpression of AcsHSP reduces viral accumulation. Mechanistically, CP is degraded via autophagy. Both AcsHSP and AcDNAJB13 interact with the autophagosome marker ATG8f1. However, AcsHSP strengthens CP-ATG8f1 binding, whereas AcDNAJB13 weakens it. These findings reveal distinct yet complementary mechanisms by which sHSP and DNAJB13 coordinate with autophagy to restrict viral infection.