Visceral organs including the lungs, liver, and kidneys harvested at various time periods were homogenized, lysed, and centrifuged to collect the supernatant containing cytoplasmic proteins. Isolated BMMs were treated with CM or taurolidine for 12 h and allowed to phagocytose E. coli for 1 h. Phagosomes were purified using a sucrose gradient as described previously (52 (link)), and phagosomal proteins were extracted. Equal amounts of protein extracts were separated on sodium dodecyl-polyacrylamide gels and transblotted onto nitrocellulose membranes (Schleicher & Schuell). The membrane was blocked for 1 h with 0.05% Tween-20 containing 5% nonfat milk and probed overnight at 4 °C with anti-LC3B (Abcam), anti-LAMP-1 (Sigma-Aldrich), anti-Rubicon (Cell Signaling), anti-β-tubulin (Sigma-Aldrich), anti-PDI (Cell Signaling), and anti-UNC93B (Abcam) antibodies. Blots were then incubated with horseradish-peroxidase-conjugated secondary antibodies, developed with SuperSignal chemiluminescent substrate (Pierce), and captured with an LAS-3000 imaging system (Fujifilm).