Characterization of Host Protein Prohibitin-2 Interacting With Cryptosporidium parvum Cyclophilin 23

Mengfei Xu1, Qi Feng1, Xichen Zhang1

  • 1State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University, Changchun 130062, China, jlu.edu.cn.

Insights

This study identifies Prohibitin-2 (PHB2) as a host protein interacting with Cryptosporidium parvum Cyclophilin 23 (CpCyP23). PHB2 expression influences C. parvum infection, offering potential targets for anti-parasitic strategies.

Area of Science:

  • Parasitology
  • Molecular Biology
  • Cell Biology

Background:

  • Cryptosporidium parvum causes significant diarrheal disease globally.
  • Host-parasite interactions are critical for C. parvum infection.
  • CpCyP23, a secreted C. parvum protein, is involved in parasite development, but its host interactions are unknown.

Purpose of the Study:

  • To identify host cell proteins interacting with CpCyP23.
  • To investigate the role of identified host-parasite interactions in C. parvum infection.
  • To explore potential therapeutic targets against C. parvum.

Main Methods:

  • Pull-down assays with mass spectrometry to screen for interacting proteins.
  • Co-immunoprecipitation (Co-IP) and bimolecular fluorescence complementation (BiFC) to validate interactions.
  • Immunofluorescence (IF) for subcellular localization.
  • siRNA knockdown and overexpression for functional analysis.

Main Results:

  • Prohibitin-2 (PHB2) was identified as a CpCyP23 interacting partner.
  • Interaction and cytoplasmic colocalization of CpCyP23 and PHB2 were confirmed.
  • PHB2 mRNA levels increased significantly post-infection.
  • PHB2 expression levels positively correlated with C. parvum infection burden.

Conclusions:

  • CpCyP23 interacts with host protein PHB2.
  • PHB2 is a key host factor influencing C. parvum infection.
  • This interaction provides a potential target for novel anti-C. parvum strategies.

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