Objectives: Human papillomavirus (HPV) type 58 is the second most prevalent virus infection among Chinese women. To develop an HPV58 vaccine that combines both prophylactic and therapeutic functions, we generate a chimeric virus-like particle (cVLP). Methods: The cVLPs contain both whole length L1 and parts of E7 peptides either from E7 amino acids (aa) 50 to aa72 or from E7 aa4 to aa12. The HPV58 L1-E7(aa50) (72) and L1-E7(aa4-12) fusion proteins were revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and confirmed by Western blot (Supplementary Digital Content 1, http://links.lww.com/IGC/A40, which shows alignment of the protein sequence between HPV58 L1-E7(aa50-72/4-12) and standard sequence). Protein folding and location of cVLPs were identified by transmission electron microscope. The immunogenicity of the fusion protein was tested by enzyme-linked immunospot assay. Results: Transmission electron microscope showed that the fusion protein formed cVLPs by self-assembly and the majority of particles located in the nucleus of the sf-9 insect cells. The cVLPs displayed a strong ability to agglutinate erythrocytes, which is distinguished from the parental VLPs. In addition, the purified HPV58 L1-E7(aa50-72) or L1-E7(aa4-12) fusion protein induced significant numbers of interferon gamma-expressing E7(aa50-72)(-) or E7(aa4-12)(-) specific CD8(+) T cells. Discussion: Our results indicate that the insertion of the E7(aa50-72) or E7(aa4-12) peptides behind L1 did not disrupt the assembly of cVLPs and provided potent immunogenicity and bioactivity, which created a powerful basis for further preparations of HPV58 vaccines with prophylactic and therapeutic effects for the treatment of HPV58-related diseases including cervical cancer.