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However, coiled coils lack features typical of protein\u2013protein interaction sites, and it is therefore challenging to understand how M proteins achieve specific binding, for example, with the human antimicrobial peptide LL-37, leading to its neutralization. The crystal structure of a complex of LL-37 with M87 protein, an antigenic M protein variant from a strain that is an emerging threat, revealed a novel interaction mode. The M87 coiled coil unfurled and asymmetrically exposed its hydrophobic core to capture LL-37. A single LL-37 molecule was bound by M87 in the crystal, but in solution additional LL-37 molecules were recruited, consistent with a \u2018protein trap\u2019 neutralization mechanism. The interaction mode visualized crystallographically was verified to contribute significantly to LL-37 resistance in an M87 Strep A strain and was identified to be conserved in a number of other M protein types that are prevalent in human populations. Our results provide specific detail for therapeutic inhibition of LL-37 neutralization by M proteins.\n                  <\/jats:p>","DOI":"10.7554\/elife.77989","type":"journal-article","created":{"date-parts":[[2022,5,30]],"date-time":"2022-05-30T07:15:17Z","timestamp":1653894917000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.77989","source":"Crossref","is-referenced-by-count":7,"title":["An M protein coiled coil unfurls and exposes its hydrophobic core to capture LL-37"],"prefix":"10.7554","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6034-8445","authenticated-orcid":true,"given":"Piotr","family":"Kolesinski","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0168r3w48","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Chemistry & Biochemistry, University of California, San Diego","place":["La Jolla, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kuei-Chen","family":"Wang","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0168r3w48","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Chemistry & Biochemistry, University of California, San Diego","place":["La Jolla, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6338-4767","authenticated-orcid":true,"given":"Yujiro","family":"Hirose","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0168r3w48","id-type":"ROR","asserted-by":"publisher"}],"name":"Division of Host-Microbe Systems and Therapeutics, Department of Pediatrics, University of California, San Diego","place":["La Jolla, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3847-0422","authenticated-orcid":true,"given":"Victor","family":"Nizet","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0168r3w48","id-type":"ROR","asserted-by":"publisher"}],"name":"Division of Host-Microbe Systems and Therapeutics, Department of Pediatrics, University of California, San Diego","place":["La Jolla, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0254-5218","authenticated-orcid":true,"given":"Partho","family":"Ghosh","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0168r3w48","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Chemistry & Biochemistry, University of California, San Diego","place":["La Jolla, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"4374","published-online":{"date-parts":[[2022,6,21]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1107\/S0907444912001308","article-title":"Towards automated crystallographic structure refinement with phenix.refine","volume":"68","author":"Afonine","year":"2012","journal-title":"Acta Crystallographica. 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