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Here, we reveal the structure and host interactome of the\n                    <jats:italic>Streptococcus pyogenes<\/jats:italic>\n                    nuclease A (SpnA). We characterize the structure and dynamics of SpnA using hydrogen-deuterium exchange mass spectrometry and single-particle electron cryo microscopy, yielding the first structural insights to SpnA. This allowed us to identify an additional oligonucleotide-binding domain, whose flexible structure may play an important function in nucleolytic activity. Affinity-pulldown mass spectrometry identified the complement system membrane attack complex (MAC) C5b67 components as key interactors. Cross-linking mass spectrometry combined with integrative modeling identified the binding interfaces between SpnA and C5b67. These interfaces are conserved among genetically diverse\n                    <jats:italic>S. pyogenes<\/jats:italic>\n                    strains. Interaction between SpnA and C5b67 is suggested to prevent the assembly of a functional MAC. Our findings uncover a novel function of SpnA in complement inhibition, and identifies new potential targets to prevent and treat\n                    <jats:italic>S. pyogenes<\/jats:italic>\n                    infections.\n                  <\/jats:p>","DOI":"10.1038\/s42003-026-10956-9","type":"journal-article","created":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T14:24:05Z","timestamp":1790173445000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Molecular mechanism of complement interference by Streptococcus pyogenes nuclease A"],"prefix":"10.1038","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0009-0007-1559-9967","authenticated-orcid":false,"given":"Isabella","family":"A. 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