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Localization characteristics of cell wall synthesis protein Wag31 and penicillin binding protein C in Clavibacter

Chengxuan Yu1, Xiaoli Xu1, Jia Shi1

  • 1State Key Laboratory of Agricultural and Forestry Biosecurity, MARA Key Laboratory of Surveillance and Management for Plant Quarantine Pests, Beijing Key Laboratory of Seed Disease Testing and Control, College of Plant Protection, China Agricultural University, Beijing 100193, China.

Cell Surface (Amsterdam, Netherlands)
|September 22, 2025
PubMed

Insights

CmWag31 protein interacts with CmPBPC, crucial for bacterial cell division and wall synthesis. Mutations affect localization, with species-specific differences observed between Clavibacter michiganensis and E. coli.

Area of Science:

  • Microbiology
  • Bacterial Cell Biology
  • Protein Interactions

Background:

  • DivIVA family proteins, including CmWag31 in Clavibacter michiganensis, are vital for bacterial cell wall peptidoglycan synthesis and cell division.
  • Penicillin-binding protein C (CmPBPC) deletion mutants are known to impact bacterial division and cell wall synthesis.
  • Previous studies confirmed an interaction between CmWag31 and CmPBPC.

Purpose of the Study:

  • To systematically analyze the localization characteristics of CmWag31 and its interaction with CmPBPC.
  • To investigate the functional impact of CmWag31 mutations on localization in different bacterial species.
  • To explore species-specific differences in the CmWag31-CmPBPC interaction and function.

Main Methods:

  • Investigated protein interaction domains between CmWag31 and CmPBPC using biochemical assays.
  • Performed co-localization studies of CmWag31 and CmPBPC in Clavibacter michiganensis and Escherichia coli.
  • Analyzed the localization of CmWag31 mutants (R19A, R19C, A99T, A102T) in E. coli and C. michiganensis.

Main Results:

  • CmWag31 interacts with the transglycosylase (TG) and transpeptidase (TP) domains of CmPBPC, while CmPBPC interacts with the NTD region of CmWag31.
  • CmWag31 and CmPBPC co-localize at bacterial growth tips in both C. michiganensis and E. coli.
  • Specific CmWag31 mutations (R19A, R19C, A99T, A102T) cause abnormal localization in E. coli, and the CmWag31A102T mutation leads to diffuse localization in C. michiganensis.
  • The CmWag31A102T mutation's localization and co-localization with CmPBPC show discrepancies between the two species.
  • Overexpression of CmPBPC restores diffused CmWag31A102T localization in C. michiganensis but not in E. coli.

Conclusions:

  • CmWag31 and CmPBPC interact and co-localize at bacterial growth sites, playing a role in cell division and wall synthesis.
  • Mutations in CmWag31 disrupt its proper localization, with species-specific variations observed.
  • CmPBPC from C. michiganensis may not fully function in E. coli, suggesting species-specific differences in protein function and interaction.
Keywords:
Clavibacter michiganensisCo-localizationPBPCWag31

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