Coxiella burnetii inhibits host immunity by a protein phosphatase adapted from glycolysis. | Academic Article individual record
abstract

Coxiella burnetii is a bacterial pathogen that replicates within host cells by establishing a membrane-bound niche called the Coxiella-containing vacuole. Biogenesis of this compartment requires effectors of its Dot/Icm type IV secretion system. A large cohort of such effectors has been identified, but the function of most of them remain elusive. Here, by a cell-based functional screening, we identified the effector Cbu0513 (designated as CinF) as an inhibitor of NF-B signaling. CinF is highly similar to a fructose-1,6-bisphosphate (FBP) aldolase/phosphatase present in diverse bacteria. Further study reveals that unlike its ortholog from Sulfolobus tokodaii, CinF does not exhibit FBP phosphatase activity. Instead, it functions as a protein phosphatase that specifically dephosphorylates and stabilizes IB. The IB phosphatase activity is essential for the role of CinF in C. burnetii virulence. Our results establish that C. burnetii utilizes a protein adapted from sugar metabolism to subvert host immunity.

authors
publication outlet

Proc Natl Acad Sci U S A

author list (cited authors)
Zhang, Y., Fu, J., Liu, S., Wang, L., Qiu, J., van Schaik, E. J., ... Luo, Z.
publication date
2022
keywords
  • NF-kappa B
  • Bacterial Proteins
  • Humans
  • Vero Cells
  • Signal Transduction
  • Nf-κb
  • HEK293 Cells
  • Animals
  • Chlorocebus Aethiops
  • Virulence Factors
  • Hela Cells
  • Coxiella Burnetii
  • Type Iv Secretion
  • Effectors
  • Protein Phosphatase
  • Phosphoprotein Phosphatases
  • Q Fever
PubMed ID
34930823
identifier
604653SE
Digital Object Identifier (DOI)
start page
e2110877119
volume
119
issue
1