pneumoniae infection has long been a mystery . Subsequent to cytadherence, M. pneumoniae is believed to cause disease in part through the generation of peroxide  and the induction of inflammatory reaction including cytokine Selleck ASP2215 productions (e.g. IL-8, TNF-α, and IL-1β) . Simultaneously, autoimmunity developed after M. pneumoniae infection likely contributes to the extrapulmonary complications. For example, anti-GM1 and galactocerebroside antibodies are the primary autoantibodies implicated in the www.selleckchem.com/products/ag-881.html ascending paralysis of Guillain-Barre syndrome and in encephalitis associated with M. pneumoniae[5, 6]. Although
toxin had not been considered as part of the M. pneumoniae repertoire in previous studies, recent Selleckchem LY333531 evidence suggested otherwise. A newly identified exotoxin of M. pneumoniae, named community-acquired respiratory distress syndrome toxin (CARDS TX), which has ADP-ribosylating and vacuolating activity, has been
suggested to be responsible for eliciting extensive vacuolization and ciliostasis of host cells . Thus, the pathophysiology of M. pneumoniae infection is likely to be complex and multifactorial, and the underlying molecular mechanisms should involve a large number of genes/proteins participating in various biological pathways [3, 8, 9]. High-throughput technologies including genomics and proteomics can comprehensively and quantitatively decipher gene/protein expression, and therefore, are useful tools in the study of complex systems under the influence of biological perturbations, such as pathogen-host interaction . Previously, using a proteomic approach, we had analyzed M. pneumoniae-induced protein expression profile using whole cell lysates, and identified the redox regulatory pathway as a key target during M. pneumoniae infection . However, as noted above, N-acetylglucosamine-1-phosphate transferase M. pneumoniae-induced immune response is important for M. pneumoniae pathogenesis, and many factors involved in the immune response, such as the cytokines, are so-called secretory proteins, which are part of the “secretome” . Secretome
proteins include extracellular matrix proteins, growth factors, cytokines and hormones, and other soluble mediators. It is known that secretory proteins are important for many physiological processes [11, 12]. For example, the matrix metalloproteinases (MMPs), as extracellular matrix-degrading enzymes, are essential regulators of the cell’s microenvironment governing cell fate and function, such as cell migration, proliferation, apoptosis, invasion and development . Moreover, changes in secretory proteins can reflect different conditions of the cells or tissues. For instance, Lietzen et al. revealed dramatic changes in secretome of macrophages, such as robust secretion of different danger-associated molecular patterns (DAMP), in response to influenza A infection . Arturo et al.