Integrated immunoreactivity analysis of MHC-I epitopes derived from the Marburg virus glycoprotein
4 affiliations
- 1Department of Immunology, The Key Laboratory of Bio-hazard Damage and Prevention Medicine, Basic Medicine School, Air-Force Medical University (the Fourth Military Medical University)
- 2Department of Rehabilitation, Tangdu Hospital, Air-Force Medical University (the Fourth Military Medical University)
- 3Military Medical Innovation Center, The Fourth Military Medical University
- 4School of Biomedical Sciences, Li Ka Shing Faculty of Medicine, The University of Hong Kong
Abstract
Introduction: 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 ⁺ 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.
Methods: 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-γ secretion in mouse splenocytes was then measured by ELISpot, serum IgG by ELISA, and CD8 ⁺ T cell cytokine production by flow cytometry.
Results: 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-γ responses. In addition, serum from GP-immunized mice contained IgG that bound the corresponding linear peptide sequences.
Conclusion: 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.
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BibTeX
@article{yang2026integrated,
title = {{Integrated immunoreactivity analysis of MHC-I epitopes derived from the Marburg virus glycoprotein}},
author = {Yulin Yang and Jing Wang and Enqi Guan and Hengzheng Wei and Yubo Sun and Jianchang Li and Yuxuan Zhang and Hao-Bo Kang and Zhenchi Fang and Jierui Zhao and Peiyuan Gao and Binjie Yao and Zhikui Li and Yongkai Wang and Yun Zhang and Chunmei Zhang and Yuanjie Sun and Rui Liu and Kun Yang and Xiyang Zhang and Dongbo T. Jiang},
journal = {Frontiers in Immunology},
year = {2026},
month = oct,
doi = {10.3389/fimmu.2026.1902130},
url = {https://www.frontiersin.org/articles/10.3389/fimmu.2026.1902130/full},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Integrated immunoreactivity analysis of MHC-I epitopes derived from the Marburg virus glycoprotein
AU - Yulin Yang
AU - Jing Wang
AU - Enqi Guan
AU - Hengzheng Wei
AU - Yubo Sun
AU - Jianchang Li
AU - Yuxuan Zhang
AU - Hao-Bo Kang
AU - Zhenchi Fang
AU - Jierui Zhao
AU - Peiyuan Gao
AU - Binjie Yao
AU - Zhikui Li
AU - Yongkai Wang
AU - Yun Zhang
AU - Chunmei Zhang
AU - Yuanjie Sun
AU - Rui Liu
AU - Kun Yang
AU - Xiyang Zhang
AU - Dongbo T. Jiang
PY - 2026
DA - 2026/10/06
JO - Frontiers in Immunology
DO - 10.3389/fimmu.2026.1902130
UR - https://www.frontiersin.org/articles/10.3389/fimmu.2026.1902130/full
AB - Introduction: 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 ⁺ 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. Methods: 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-γ secretion in mouse splenocytes was then measured by ELISpot, serum IgG by ELISA, and CD8 ⁺ T cell cytokine production by flow cytometry. Results: 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-γ responses. In addition, serum from GP-immunized mice contained IgG that bound the corresponding linear peptide sequences. Conclusion: 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.
SN - 1664-3224
ER -