{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T04:54:11Z","timestamp":1791262451201,"version":"4.1.0"},"reference-count":52,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T00:00:00Z","timestamp":1791244800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["82203510"],"award-info":[{"award-number":["82203510"]}],"id":[{"id":"10.13039\/501100001809","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>Introduction<\/jats:title>\n                    <jats:p>\n                      Marburg virus (MARV) is a hemorrhagic fever virus, and its glycoprotein (GP) represents an important target for vaccine research. MHC class I (MHC-I)-restricted T cell epitopes are critical for inducing cytotoxic CD8\n                      <jats:sup>+<\/jats:sup>\n                      T cell responses. In this study, we aimed to identify MHC-I-restricted T cell epitopes derived from the MARV Angola strain GP through an integrated bioinformatics and experimental approach.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      We retrieved the MARV Angola strain GP sequence and divided it into 673 overlapping 9-mer peptides. By integrating five computational prediction algorithms, immunogenicity scoring tools and BLASTp conservation analysis, we screened 9-mer peptides from the MARV Angola GP. Molecular docking was performed with MHC-I structures using HPEPDOCK and molecular dynamics (MD) analysis. Bidirectional hierarchical clustering was used to analyze binding similarity across MHC-I molecules. Mutations identified in epitope regions were tested for their effect on affinity. Toxicity and allergenicity of the epitopes were predicted using dedicated tools. Finally, BALB\/c and C57BL\/6 mice were immunized with a DNA vaccine encoding MARV GP. IFN-\u03b3 secretion in mouse splenocytes was then measured by ELISpot, serum IgG by ELISA, and CD8\n                      <jats:sup>+<\/jats:sup>\n                      T cell cytokine production by flow cytometry.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Among 673 GP peptides, eight epitopes (GAFFLYDRI, REGDMFPFL, DMFPFLDGL, NENDCDAEL, AGLSWIPFF, NQNNLVCRL, TGWGLGGKW, SDWGVLTNL) were predicted to exhibit high-affinity MHC-I binding, strong immunogenicity, and intraspecies conservation. Bidirectional hierarchical clustering analysis, molecular docking, sequence alignment, and toxicity\/allergenicity predictions suggested binding across selected alleles, structural stability, limited impact from identified mutations, and low predicted toxicity. In subsequent ELISpot validation, eight epitopes elicited strong IFN-\u03b3 responses. In addition, serum from GP-immunized mice contained IgG that bound the corresponding linear peptide sequences.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>An integrated computational-experimental pipeline identified eight conserved, immunogenic MHC-I epitopes from MARV GP. These selected epitopes may serve as promising candidates for future vaccine design.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fimmu.2026.1902130","type":"journal-article","created":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T04:24:55Z","timestamp":1791260695000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Integrated immunoreactivity analysis of MHC-I epitopes derived from the Marburg virus glycoprotein"],"prefix":"10.3389","volume":"17","author":[{"given":"Yulin","family":"Yang","sequence":"first","affiliation":[{"name":"Department of Immunology, The Key Laboratory of Bio-hazard Damage and Prevention Medicine, Basic Medicine School, Air-Force Medical University (the Fourth Military Medical University)","place":["Xi\u2019an, Shaanxi, China"]},{"name":"Department of Rehabilitation, Tangdu Hospital, Air-Force Medical University (the Fourth Military Medical 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