PRIP mediates autophagic elimination of intracellular bacteria.

2014 Fiscal Year Final Research Report

• Project/Area Number: 25861757
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Functional basic dentistry
• Research Institution: Hiroshima University
• Principal Investigator: HARADA Kae 広島大学, 医歯薬保健学研究院(歯), 助教 (60432663)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: オートファジー / 細菌感染 / 微生物

Outline of Final Research Achievements

PRIP (PLC-related catalytically inactive protein) interacts with both LC3 and GABARAP which are modulators of autophagy. We previously reported that PRIP regulates autophagic pathway triggered by amino-acid starvation.
In this study, we explored autophagic pathway in PRIP-deficient (Prip-DKO) cells infected with Staphylococcus aureus. LC3-positive autophagosome-like vacuoles (SAcAVs) in Prip-DKO cells enclosed more S. aureus than wild-type cells, suggesting that S. aureus proliferates in the SAcAVs of Prip-DKO cells. Then, autophagic flux was analyzed using an RFP-GFP-tagged LC3 and a lysosomal dye. Autophagosome maturation, the fusion between autophagosome and lysosome, was significantly inhibited in Prip-DKO cells.
These data indicate that PRIP mediates the fusion of SAcAVs with lysosomes and is a novel autophagy modulator which combats infection of pathogenic bacteria in host cells.

Free Research Field

歯科薬理学