Hemolymph protein profiles of subterranean termite Reticulitermes flavipes challenged with methicillin resistant Staphylococcus aureus or Pseudomonas aeruginosa

When the subterranean termite Reticulitermes flavipes is fed heat-killed methicillin resistant Staphylococcus aureus (MRSA) or Pseudomonas aeruginosa, the termite produces proteins with antibacterial activity against the inducer pathogen in its hemolymph. We used a proteomic approach to characterize the alterations in protein profiles caused by the inducer bacterium in the hemolymph of the termite. Nano-liquid chromatography-tandem mass spectrometry analysis identified a total of 221 proteins and approximately 70% of these proteins could be associated with biological processes and molecular functions. Challenges with these human pathogens induced a total of 57 proteins (35 in MRSA-challenged, 16 in P. aeruginosa-challenged, and 6 shared by both treatments) and suppressed 13 proteins by both pathogens. Quasi-Poisson likelihood modeling with false discovery rate adjustment identified a total of 18 and 40 proteins that were differentially expressed at least 2.5-fold in response to MRSA and P. aeruginosa-challenge, respectively. We selected 7 differentially expressed proteins and verified their gene expression levels via quantitative real-time RT-PCR. Our findings provide an initial insight into a putative termite immune response against MRSA and P. aeruginosa-challenge.