HPV16-E7-43-57, HPV

GQAEPDRAHYNIVTF is a 15-amino acid peptide derived from the E7 oncoprotein of Human Papillomavirus type 16 (HPV16 E7 43–57). This sequence is frequently included in immunogen designs as a cytotoxic T lymphocyte (CTL) epitope component, often within multiepitope HPV vaccines. In silico and vaccine design studies identify GQAEPDRAHYNIVTF as an immunodominant CTL epitope for HPV16 E7.

Human papilloma virus type 16 (HPV 16) oncoprotein E7 (HPV16-E743-57: GQAEPDRAHY- NIVTF), Self-Assembling Peptide Epitopes (SAPEs) can be used as Novel Platform for Anticancer Vaccination. The results showed that the SAPEs were able to form nanostructures with a diameter from 20 to 200 nm. The SAPEs adjuvanted with CpG induced and expanded antigen-specific CD8+ T cells in mice. Furthermore, tumor-bearing mice vaccinated with SAPEs harboring the HPV E743-57 peptide exhibited delayed tumor growth and increased survival compared to sham-treated mice.

Functional Role & Mechanism

• Antigenic Epitope: This peptide represents a class I MHC-restricted CTL epitope within HPV16 E7 used to drive antigen-specific CD8⁺ T cell responses.

• Immune Activation: When properly presented on antigen-presenting cells (APCs), it may stimulate CTLs to recognize HPV16-infected cells, contributing to anti-tumor immunity.

• Self-Assembly Context: As a self-assembling epitope, the peptide may be engineered to form nanofibers, nanoparticles, or co-assembled scaffolds, which can enhance immunogenicity by multivalent presentation and slow release.

Applications

• Therapeutic Vaccine Design: As a component of peptide vaccines targeting HPV16-associated cervical cancers or precancerous lesions.

• Immunological Assays: Use in ELISPOT, intracellular cytokine staining (ICS), and tetramer staining to monitor E7-specific T cell responses.

• Nanoparticle & Biomaterial Constructs: Conjugation to self-assembling scaffolds or carrier proteins to enhance stability, uptake, and immune potency.

• Preclinical Models: Testing efficacy of vaccine formulations or delivery systems in mouse tumor models or humanized systems.

References

• Kayyal et al., “In Silico Design and Immunological Studies … HPV16 E7 (216GQAEPDRAHYNIVTF)” — identifies this peptide as a predicted immunogenic epitope in multiepitope vaccine constructs.

• Namvar et al., “Development of HPV16,18,31,45 E5 and E7 peptides” — includes GQAEPDRAHYNIVTF among evaluated E7 peptide candidates.

HPV16-E7-43-57, HPV is a 15-residue synthetic peptide with the sequence Gly-Gln-Ala-Glu-Pro-Asp-Arg-Ala-His-Tyr-Asn-Ile-Val-Thr-Phe. C-terminal amidation removes the terminal carboxylate charge. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence.

• LC-MS/HPLC analytical method development
• sequence-specific assay controls

Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions.