Scholarlink

Background <p>The tick <i>Haemaphysalis longicornis</i> is a major vector for several zoonotic pathogens, including <i>Rickettsia heilongjiangensis</i>. Small heat-shock proteins (sHSPs) are critical for stress responses and host–pathogen interactions. Among them, the <i>HSP20</i> gene was found upregulated during rickettsial infection, whereas its specific function at the host–pathogen interface remains undefined.</p> Methods <p>The full length of the <i>HSP20</i> gene (<i>HlHSP20</i>) and its expression profile was characterized in <i>H. longicornis</i>, and RNA interference (RNAi) was used to knockdown <i>HlHSP20</i>, followed by the quantification of <i>R. heilongjiangensis</i> proliferation. Proteins from <i>R. heilongjiangensis</i> interacting with HlHSP20 were identified using GST pulldown coupled with liquid chromatography–tandem mass spectrometry (LC–MS/MS) and validated by yeast two-hybrid (Y2H) assays.</p> Results <p>HlHSP20 is a conserved, non-transmembrane intracellular <i>sHSP</i> with a αB-crystallin domain, showing the highest expression in egg and larval stages. The knockdown of HlHSP20 significantly promoted the proliferation of <i>R. heilongjiangensis</i>, and interaction screening revealed that HlHSP20 specifically binds to the 50S ribosomal protein L14 (RhRPL14) of <i>R. heilongjiangensis</i>.</p> Conclusions <p>The present study demonstrates that HlHSP20 acts as a host restriction factor against <i>R. heilongjiangensis</i> in <i>H. longicornis</i>, likely through a direct interaction with the pathogen ribosome protein. This work unveils a novel component of the antimicrobial defense of ticks and identifies HlHSP20 as a potential target for disrupting rickettsial transmission.</p> Graphical Abstract <p></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

Haemaphysalis longicornis HSP20 inhibits Rickettsia heilongjiangensis replication by targeting the pathogen 50S ribosomal protein

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年4月8日

查看全文
  • Yuchao Zhang,
  • Lian-Feng Li,
  • Wen-Jie Zhu,
  • Tingwei Pei,
  • Han Wang,
  • Xiujie Liang,
  • Yunsheng Tang,
  • Chunyuan Wang,
  • Songbo Zhang,
  • Wu-Chun Cao,
  • Zhijun Yu,
  • Tianhong Wang

摘要

Background

The tick Haemaphysalis longicornis is a major vector for several zoonotic pathogens, including Rickettsia heilongjiangensis. Small heat-shock proteins (sHSPs) are critical for stress responses and host–pathogen interactions. Among them, the HSP20 gene was found upregulated during rickettsial infection, whereas its specific function at the host–pathogen interface remains undefined.

Methods

The full length of the HSP20 gene (HlHSP20) and its expression profile was characterized in H. longicornis, and RNA interference (RNAi) was used to knockdown HlHSP20, followed by the quantification of R. heilongjiangensis proliferation. Proteins from R. heilongjiangensis interacting with HlHSP20 were identified using GST pulldown coupled with liquid chromatography–tandem mass spectrometry (LC–MS/MS) and validated by yeast two-hybrid (Y2H) assays.

Results

HlHSP20 is a conserved, non-transmembrane intracellular sHSP with a αB-crystallin domain, showing the highest expression in egg and larval stages. The knockdown of HlHSP20 significantly promoted the proliferation of R. heilongjiangensis, and interaction screening revealed that HlHSP20 specifically binds to the 50S ribosomal protein L14 (RhRPL14) of R. heilongjiangensis.

Conclusions

The present study demonstrates that HlHSP20 acts as a host restriction factor against R. heilongjiangensis in H. longicornis, likely through a direct interaction with the pathogen ribosome protein. This work unveils a novel component of the antimicrobial defense of ticks and identifies HlHSP20 as a potential target for disrupting rickettsial transmission.

Graphical Abstract