{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T06:15:48Z","timestamp":1778652948064,"version":"3.51.4"},"reference-count":68,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T00:00:00Z","timestamp":1778630400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100014718","name":"Innovative Research Group Project of the National Natural Science Foundation of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100014718","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Immunol."],"abstract":"<jats:sec>\n                    <jats:title>Background and aims<\/jats:title>\n                    <jats:p>The deposition of \u03b2-amyloid (A\u03b2) in the cerebral cortex and hippocampus is a key pathological hallmark of Alzheimer\u2019s disease (AD). Previous studies have shown that ASC specks released by activated microglia can bind to A\u03b2 and promote its aggregation, thereby accelerating AD progression. However, the specific mechanisms underlying this interaction remain poorly understood. This study aims to identify the interaction sites between ASC and A\u03b2, design a vaccine targeting these sites, and evaluate its immunogenicity and therapeutic efficacy.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      The interaction regions between ASC and A\u03b2 were identified using pull-down and ELISA assays. Four types of nanoparticle carriers were purified using a prokaryotic expression system, and two peptides targeting the interaction sites were synthesized\n                      <jats:italic>in vitro<\/jats:italic>\n                      . These peptides were conjugated to the carriers via the SpyCatcher-SpyTag system. C57BL\/6J mice were immunized with the constructed nanoparticles, and the immunogenicity of the vaccines was assessed by ELISA, while safety was evaluated by ELISpot. Serum antibodies were purified for further functional analysis.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      Pull-down and ELISA results demonstrated that the C-terminal region of A\u03b2, particularly residues 29-42, and the pyrin domain (PYD) of ASC are key regions involved in binding. Eight nanoparticle vaccines carrying A\u03b2 C-terminal epitopes were successfully prepared. Among them, the Ferritin-based A\u03b2 vaccine induced a potent immune response targeting the A\u03b2-ASC interaction site without activating A\u03b2-specific T-cell responses.\n                      <jats:italic>In vitro<\/jats:italic>\n                      functional assays confirmed that the purified antibodies effectively disrupted A\u03b2-ASC binding, inhibited A\u03b2 aggregation, and subsequently reduced its neurotoxicity.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion<\/jats:title>\n                    <jats:p>Our findings indicate that the interaction site between ASC and A\u03b2 is located within amino acids 29-42 of A\u03b2. Vaccines designed based on this site, Ferritin-A\u03b229-35-3copy and Ferritin-A\u03b236-42-3copy, effectively induced antibody production. The resulting antibodies suppressed A\u03b2 aggregation and the neurotoxicity of A\u03b2 oligomers. These data suggest that the A\u03b2-ASC interaction site may represent a potential target for AD therapy.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fimmu.2026.1748748","type":"journal-article","created":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T05:57:41Z","timestamp":1778651861000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["The inhibition of the A\u03b2-ASC interaction site suppresses \u03b2-amyloid aggregation and cytotoxicity"],"prefix":"10.3389","volume":"17","author":[{"given":"Lan","family":"Zhao","sequence":"first","affiliation":[{"name":"National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University","place":["Changchun, China"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xue","family":"Xia","sequence":"additional","affiliation":[{"name":"National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin 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