MYCOLab Ai Logo - gold and army green

Phospholipase PlcH is involved in the secretion of cell wall glycoproteins and contributes to the host immune response of Aspergillus fumigatus

Summary

Researchers discovered that an enzyme called PlcH helps a dangerous mold called Aspergillus fumigatus release protective proteins into its cell wall. These proteins help the fungus survive and evade the immune system. When scientists removed the gene for PlcH, the fungus became weaker and more vulnerable to both antifungal drugs and immune cells, suggesting PlcH could be a target for new antifungal treatments.

Background

Aspergillus fumigatus is a major fungal pathogen causing invasive aspergillosis with high mortality rates. The fungal cell wall contains glycoproteins that form the outer protective layer, but the mechanisms of how these glycoproteins are secreted to the cell wall remain unclear.

Objective

To identify and characterize the role of phospholipase PlcH in the secretion of GPI-anchored cell wall proteins (GPI-CWPs) from the plasma membrane of A. fumigatus and its contribution to cell wall integrity and host immune response.

Results

PlcH was confirmed as a phospholipase C that specifically hydrolyzes phosphate ester bonds to release GPI-CWPs from the membrane. Deletion of plcH resulted in abnormal conidiation, polar abnormalities, increased antifungal drug sensitivity, and altered cell wall composition with reduced mannoproteins and β-glucans.

Conclusion

PlcH represents a newly discovered secretory pathway for GPI-CWPs in A. fumigatus that is crucial for cell wall integrity and virulence. These findings provide insight into fungal cell wall assembly and identify potential new targets for antifungal therapies and diagnosis.
  • Published in:mLife,
  • Study Type:Experimental Research,
  • Source: PMID: 39744093, DOI: 10.1002/mlf2.12146
Scroll to Top