Data of sadA role in Staph pathogenicity

Aromatic amino acid decarboxylase is prevalent in bacteria associated with food fermentation and human commensal. This enzyme, called SadA, is reported to be found in various staphylococcal species and might contribute to colonization and host-bacteria interactions. However, the role of SadA in staphylococcal pathogenicity related to infection is understudied. This study aims to evaluate the role of <i>sadA</i> in the pathogenicity of <i>Staphylococcus pseudintermedius</i> ED99 and <i>Staphylococcus aureus</i> USA300 LAC using invertebrate and mammalian infection models. We performed a <i>Galleria mellonella</i> survival assay, a mouse infection model, and analysis of trace amine levels using high-performance liquid chromatography (HPLC). In addition, cytokine production in human monocyte cells (Monomac-6) exposed to trace amines was also measured. The results showed that <i>sadA</i> expression increased the virulence of <i>S. pseudintermedius</i> ED99 on <i>G. mellonella</i> when supplemented with aromatic amino acids, but in a mouse model, no significant differences were found in infection rates, bacterial burdens, or trace amine production between strains with and without <i>sadA</i>. Moreover, tryptamine only induced IL-10 production in Monomac-6 cells at high concentration (50 μg/ml). In conclusion, <i>sadA </i>does not play a significant role in staphylococcal pathogenicity in mammalian models due to substrate limitations in the host.