Author Response: Structural Basis of Malodor Precursor Transport in the Human Axilla

The study identified the crystal structure of a transporter protein in Staphylococcus hominis involved in underarm odor production. Functional assays in E. coli and proteoliposomes suggested that the transporter's flexible binding site allows recognition of various peptide derivatives. Reviewers recommended knockout experiments to confirm if this transporter is the primary route for S-Cys-Gly-3M3SH uptake. Additional data showed that di- and tripeptides inhibit 3M3SH production, supporting the transporter's role. Despite genetic manipulation limitations, the study concluded that SH1446 is the major transporter for Cys-Gly-3M3SH in S. hominis. The transporter had a turnover number of approximately 10 per minute and recognized natural peptides more favorably than modified ones, with the addition of a thioalcohol group impairing transport.