Structural and functional analysis of TREM2 interactions with amyloid beta reveal molecular mechanisms that drive phagocytosis of oligomeric amyloid beta

Our results indicate that TREM2 uses the hydrophobic site (consisting of the CDR1, CDR2, and CDR3 loops) to engage the N-terminal region of the Ab42 peptide to drive phagocytosis of oAb42. They also suggest that therapeutics that either directly bind or allosterically alter the hydrophobic site on TREM2 should modulate TREM2 signaling as potential AD treatments.