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Consistent with this view, monoclonal antibodies against IsaA were previously shown to be protective against<jats:italic>S<\/jats:italic>.<jats:italic>aureus<\/jats:italic>infections in mouse models. Further, patients with the genetic blistering disease epidermolysis bullosa (EB) displayed high IsaA-specific IgG levels that could potentially be protective. Yet, mice actively immunized with IsaA were not protected against<jats:italic>S<\/jats:italic>.<jats:italic>aureus<\/jats:italic>infection. The present study was aimed at explaining these differences in IsaA-specific immune responses. By epitope mapping, we show that the protective human monoclonal antibody (humAb) 1D9 recognizes a conserved 62-residue N-terminal domain of IsaA. The same region of IsaA is recognized by IgGs in EB patient sera. Further, we show by immunofluorescence microscopy that this N-terminal IsaA domain is exposed on the<jats:italic>S<\/jats:italic>.<jats:italic>aureus<\/jats:italic>cell surface. In contrast to the humAb 1D9 and IgGs from EB patients, the non-protective IgGs from mice immunized with IsaA were shown to predominantly bind the C-terminal domain of IsaA. Altogether, these observations focus attention on the N-terminal region of IsaA as a potential target for future immunization against<jats:italic>S<\/jats:italic>.<jats:italic>aureus<\/jats:italic>.<\/jats:p>","DOI":"10.1038\/s41598-017-08182-9","type":"journal-article","created":{"date-parts":[[2017,8,9]],"date-time":"2017-08-09T08:16:26Z","timestamp":1502266586000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Differential epitope recognition in the immunodominant staphylococcal antigen A of Staphylococcus aureus by mouse versus human IgG antibodies"],"prefix":"10.1038","volume":"7","author":[{"given":"Dennis G. A. 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