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Peer-reviewedCC BYBiology

DIA Quantitative Proteomic Analysis Reveals Early Proteomic Responses to Honeybee-Derived Melittin in Murine Breast Cancer Cells.

  • Junling Zhu1
  • Wenhua Xu2,3,4
  • He Zang2,3,4
  • Yunzhen Yang2,3,4
  • Nian Fan2,3,4
  • Yuwei Zhang2,3,4
  • Yaqin Gao2,3,4
  • Jianfeng Qiu2,3,4
  • Dafu Chen2,3,4
  • Rui Guo2,3,4
4 affiliations
  1. 1Ningbo No. 2 Hospital, Wenzhou Medical University, Ningbo 315000, China.
  2. 2National & Local United Engineering Laboratory of Natural Biotoxin, Fuzhou 350002, China.
  3. 3Apitherapy Research Institute, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
  4. 4College of Bee Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
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Abstract

Breast cancer remains a major clinical challenge because of its molecular heterogeneity, therapeutic resistance, and disease recurrence. Melittin, the principal bioactive peptide of honeybee venom, exhibits antitumor activity in multiple experimental models; however, its early proteome-wide effects in breast cancer cells remain incompletely characterized. In this study, E0771 murine mammary carcinoma cells were exposed to melittin for 15 min. Colony formation and CCK-8 assays using 0-8 μg/mL melittin showed concentration-dependent reductions in clonogenic capacity and cell viability. For DIA-based quantitative proteomic profiling, E0771 cells were treated with 4 μg/mL melittin for 15 min. Among 9748 quantified protein entries, 339 proteins met the exploratory criteria for candidate differential abundance, including 114 up-regulated and 225 down-regulated candidates. GO and KEGG analyses associated these candidate proteins with cell junctions, cytoskeletal organization, protein kinase-related functions, metabolic processes, and cell-death-associated pathways. A STRING-derived association network containing 132 nodes and 216 edges further prioritized CASP8, RPS27A, ANXA5, and PIK3CA as relatively high-connectivity candidates. Collectively, these findings describe early proteomic responses to short-term melittin exposure and provide candidate proteins and biological processes for subsequent mechanistic validation rather than establishing causal molecular mechanisms.

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Cite

BibTeXRIS
BibTeX
@article{zhu2026quantitative,
  title = {{DIA Quantitative Proteomic Analysis Reveals Early Proteomic Responses to Honeybee-Derived Melittin in Murine Breast Cancer Cells.}},
  author = {Junling Zhu and Wenhua Xu and He Zang and Yunzhen Yang and Nian Fan and Yuwei Zhang and Yaqin Gao and Jianfeng Qiu and Dafu Chen and Rui Guo},
  journal = {Biology},
  year = {2026},
  month = oct,
  doi = {10.3390/biology15191727},
  url = {https://europepmc.org/article/MED/42883400},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - DIA Quantitative Proteomic Analysis Reveals Early Proteomic Responses to Honeybee-Derived Melittin in Murine Breast Cancer Cells.
AU  - Junling Zhu
AU  - Wenhua Xu
AU  - He Zang
AU  - Yunzhen Yang
AU  - Nian Fan
AU  - Yuwei Zhang
AU  - Yaqin Gao
AU  - Jianfeng Qiu
AU  - Dafu Chen
AU  - Rui Guo
PY  - 2026
DA  - 2026/10/01
JO  - Biology
DO  - 10.3390/biology15191727
UR  - https://europepmc.org/article/MED/42883400
AB  - Breast cancer remains a major clinical challenge because of its molecular heterogeneity, therapeutic resistance, and disease recurrence. Melittin, the principal bioactive peptide of honeybee venom, exhibits antitumor activity in multiple experimental models; however, its early proteome-wide effects in breast cancer cells remain incompletely characterized. In this study, E0771 murine mammary carcinoma cells were exposed to melittin for 15 min. Colony formation and CCK-8 assays using 0-8 μg/mL melittin showed concentration-dependent reductions in clonogenic capacity and cell viability. For DIA-based quantitative proteomic profiling, E0771 cells were treated with 4 μg/mL melittin for 15 min. Among 9748 quantified protein entries, 339 proteins met the exploratory criteria for candidate differential abundance, including 114 up-regulated and 225 down-regulated candidates. GO and KEGG analyses associated these candidate proteins with cell junctions, cytoskeletal organization, protein kinase-related functions, metabolic processes, and cell-death-associated pathways. A STRING-derived association network containing 132 nodes and 216 edges further prioritized CASP8, RPS27A, ANXA5, and PIK3CA as relatively high-connectivity candidates. Collectively, these findings describe early proteomic responses to short-term melittin exposure and provide candidate proteins and biological processes for subsequent mechanistic validation rather than establishing causal molecular mechanisms.
SN  - 2079-7737
ER  -