What question did this study set out to answer?

This study aims to investigate how PRRSV NSP2 manipulates host cellular processes to enhance viral replication.

May 29, 2026

PRRSV NSP2 hijacks host lipophagy via a LIPE-PNPLA2-AMPK-MTOR axis to promote viral replication

Key Points

This study aims to investigate how PRRSV NSP2 manipulates host cellular processes to enhance viral replication.
Co-immunoprecipitation to analyze protein interactions
Use of lipid droplet and autophagy markers
Infection of HEK-293T cells with PRRSV
PRRSV NSP2 activates the LIPE-PNPLA2-AMPK-MTOR pathway, enhancing lipophagy and fatty acid availability for viral replication.
Overexpression of NSP2 significantly increases viral titers compared to controls (exact values not provided).
Inhibition of lipophagy reduces PRRSV replication levels, implying a critical role for host lipid metabolism.

Abstract

: AMPK: AMP-activated protein kinase; co-IP: co-immunoprecipitation; CQ: chloroquine; CMA: chaperone-mediated autophagy; FFA: free fatty acid; HEK-293T: human embryonic kidney 293T; hpi: hour post infection; LAMP1: lysosome associated membrane protein 1; LD: lipid droplet; LIPA/LAL: lipase A, lysosomal acid type; LIPE/HSL: lipase E, hormone sensitive type; LIRs: LC3-interacting regions; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MGLL: monoglyceride lipase; MG132: carbobenzoxyl-l-leucyl-l-leucyl-l-leucinal; MOI: multiplicity of infection; MTOR: mechanistic target of rapamycin kinase; NSPs: non-structural proteins; ORFs: open reading frames; PNPLA2/ATGL: patatin-like domain 2, triacylglycerol lipase; PRRSV: porcine reproductive and respiratory syndrome virus; SQSTM1/p62: sequestosome 1.

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