Gordon W. Laurie

This study investigates how site-specific O-glycans on lacritin influence its structure and multimerization, revealing their role in conformational flexibility and crosslinking residue positioning.

This study identifies N-104, a cleavage-potentiated form of lacritin, as a bactericidal agent that alters the transcriptome of P. aeruginosa PA14, reducing virulence, fitness, metabolism, and stress response while increasing efflux and anaerobic respiration.

This study identifies new Gal-3 ligands in tear fluid, showing that lacritin's glycoforms and spliceoforms specifically bind Gal-3, influencing its biological functions.

The paper identifies a non-lytic bactericidal mechanism in P. aeruginosa by targeting multiple transporters and transcription, leading to respiratory suppression and bacterial death.