BALF samples were sent to the Yale MS & Proteomics Resource (New Haven, CT), where they were processed and analyzed via a Label Free Quantification workflow as described by Charkoftaki et al. (25 (link)). The sample preparation was slightly modified from the 2019 protocol of Charkoftaki et al. (25 (link)) given the samples were BALF. In brief, samples were filtered through a 3-kDa Amicon Ultra filter, and the retentate was SpeedVac dried and used for downstream proteomics preparation. Dried protein pellets were reduced with DTT, alkylated with iodoacetamide, enzymatically digested with LysC and trypsin, and desalted using C18 RP microspin column. High-resolution liquid chromatography mass spectrometry (MS)/MS data were collected on an Orbitrap Fusion mass spectrometer coupled to a NanoACQUITY UPLC and analyzed using Progenesis QI (Waters, Milford, MA) and Mascot search engine. Quantitative data were normalized based on equal total amount of peptides/proteins injected on column, and positive protein identification and quantitation were based on hits with two or more unique peptides per protein. Experimental groups were compared and considered statistically significant when the FDR q value was <0.05, unless otherwise stated. IPA (Qiagen Bioinformatics) was used for further analyses.