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In this study, broilers were subjected to a 2\u2009\u00d7\u20092 factorial design with sodium selenite or yeast \u03b2-glucan selenium nanoparticles (yeast \u03b2-Glu-SeNPs) as the selenium source (0.3 mg\/kg total selenium) under thermoneutral or HS conditions. We aimed to investigate the protective effects and underlying mechanisms of yeast \u03b2-Glu-SeNPs against HS-induced muscle damage.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      HS markedly impaired growth performance and induced systemic oxidative stress and inflammation, while also compromising meat quality and disrupting postmortem glycolysis, as evidenced by reduced glycogen availability and excessive lactate accumulation. Yeast \u03b2-Glu-SeNPs significantly improved growth performance, mitigated oxidative stress and inflammation, and restored meat quality in both breast and thigh muscles. Postmortem energy metabolism was preserved, as reflected by increased muscle glycogen and glycolytic potential, reduced lactate accumulation and glycolytic enzyme activities, and a stabilized pH decline. Meanwhile, skeletal muscle Se deposition, glutathione peroxidase activity, and key selenoprotein expression were markedly enhanced. Notably, HS promoted a phenotypic shift toward fast glycolytic muscle fibers, as evidenced by increased expression of\n                      <jats:italic>MYHC2b<\/jats:italic>\n                      and Fast-MyHC (\n                      <jats:italic>P<\/jats:italic>\n                      \u2009&lt;\u20090.05), accompanied by reduced levels of\n                      <jats:italic>MYHC1<\/jats:italic>\n                      ,\n                      <jats:italic>MYHC2a<\/jats:italic>\n                      , and Slow-MyHC (\n                      <jats:italic>P<\/jats:italic>\n                      \u2009&lt;\u20090.05). This maladaptive transition was effectively reversed by yeast \u03b2-Glu-SeNPs, which favored oxidative fiber formation, characterized by the upregulation of\n                      <jats:italic>MYHC1<\/jats:italic>\n                      and\n                      <jats:italic>MYHC2a<\/jats:italic>\n                      , along with the suppression of\n                      <jats:italic>MYHC2b<\/jats:italic>\n                      (\n                      <jats:italic>P<\/jats:italic>\n                      \u2009&lt;\u20090.05). At the mitochondrial level, yeast \u03b2-Glu-SeNPs preserved ultrastructural integrity and enhanced mitochondrial function, as reflected by increased ATP content, elevated mtDNA copy number, and the upregulation of mitochondrial biogenesis-related genes, including\n                      <jats:italic>AMPK<\/jats:italic>\n                      ,\n                      <jats:italic>PGC-1\u03b1<\/jats:italic>\n                      ,\n                      <jats:italic>NRF1<\/jats:italic>\n                      , and\n                      <jats:italic>TFAM<\/jats:italic>\n                      (\n                      <jats:italic>P<\/jats:italic>\n                      \u2009&lt;\u20090.05). Correlation analysis, molecular docking, and co-immunoprecipitation demonstrated that SelO interacts with AMPK, supporting a SelO-dependent AMPK\/PGC-1\u03b1 axis that drives mitochondrial biogenesis and oxidative fiber remodeling.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>Overall, yeast \u03b2-Glu-SeNPs mitigated HS-induced muscle metabolic dysfunction and meat quality deterioration via SelO-mediated mitochondrial and myofiber reprogramming.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1186\/s40104-026-01437-4","type":"journal-article","created":{"date-parts":[[2026,7,3]],"date-time":"2026-07-03T23:01:15Z","timestamp":1783119675000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Yeast \u03b2-glucan selenium nanoparticles enhance meat quality in heat-stressed broilers via SelO-mediated mitochondrial biogenesis and oxidative myofiber remodeling"],"prefix":"10.1186","volume":"17","author":[{"given":"Weiguang","family":"Yang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chengkun","family":"Fang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiani","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Lv","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guanyu","family":"Shang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinhao","family":"Song","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yujing","family":"Tang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shusong","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rejun","family":"Fang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,7,4]]},"reference":[{"issue":"1","key":"1437_CR1","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1186\/s40104-024-01028-1","volume":"15","author":"S Al Amaz","year":"2024","unstructured":"Al Amaz S, Mishra B. 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