A patient-specific therapeutic cancer peptide vaccine composed of synthetic peptides representing tumor-specific somatic mutations selected via whole-exome/RNA sequencing and HLA typing to generate high-affinity HLA-binding peptides. Designed to prime and expand neoantigen-specific CD8+ and CD4+ T cells via dendritic cell antigen presentation, enabling recognition and killing of tumor cells expressing the targeted neoantigens.
Patient-specific synthetic neoantigen peptides are selected by tumor sequencing and HLA typing and administered to be taken up and presented by antigen-presenting cells (HLA class I/II). This primes and expands neoantigen-specific CD8+ cytotoxic and CD4+ helper T cells, enabling immune recognition and killing of tumor cells expressing the targeted mutations.
NO
INDIRECT
The vaccine primes neoantigen-specific T cells via APC presentation; activated T cells kill tumor cells presenting the neoantigen/HLA complexes (perforin–granzyme/Fas pathways). HLA-DQB1 itself is not targeted for killing.
A patient-specific therapeutic cancer peptide vaccine composed of synthetic peptides representing tumor-specific somatic mutations selected via whole-exome/RNA sequencing and HLA typing to generate high-affinity HLA-binding peptides. Designed to prime and expand neoantigen-specific CD8+ and CD4+ T cells via dendritic cell antigen presentation, enabling recognition and killing of tumor cells expressing the targeted neoantigens.
Patient-specific synthetic neoantigen peptides are selected by tumor sequencing and HLA typing and administered to be taken up and presented by antigen-presenting cells (HLA class I/II). This primes and expands neoantigen-specific CD8+ cytotoxic and CD4+ helper T cells, enabling immune recognition and killing of tumor cells expressing the targeted mutations.
NO
INDIRECT
The vaccine primes neoantigen-specific T cells that kill tumor cells presenting the mutant peptide on HLA molecules via TCR recognition and perforin/granzyme-mediated lysis; HLA-DPA1 itself is not the cytotoxic target.
A patient-specific therapeutic cancer peptide vaccine composed of synthetic peptides representing tumor-specific somatic mutations selected via whole-exome/RNA sequencing and HLA typing to generate high-affinity HLA-binding peptides. Designed to prime and expand neoantigen-specific CD8+ and CD4+ T cells via dendritic cell antigen presentation, enabling recognition and killing of tumor cells expressing the targeted neoantigens.
Patient-specific synthetic neoantigen peptides are selected by tumor sequencing and HLA typing and administered to be taken up and presented by antigen-presenting cells (HLA class I/II). This primes and expands neoantigen-specific CD8+ cytotoxic and CD4+ helper T cells, enabling immune recognition and killing of tumor cells expressing the targeted mutations.
NO
INDIRECT
The vaccine primes neoantigen-specific T cells; CD8+ T cells kill tumor cells presenting the neoantigen peptides on MHC, via perforin/granzyme or Fas–FasL. HLA-DPB1 serves as an antigen-presentation molecule and is not itself targeted for killing.
An anti-EGFR antibody–drug conjugate (ADC) with a drug–antibody ratio of 8 that couples an EGFR-specific monoclonal antibody to a high-potency DNA topoisomerase I inhibitor. After binding EGFR and internalization, it releases the topo I inhibitor to cause DNA damage and apoptosis; the antibody component may also inhibit EGFR signaling.
EGFR-targeting IgG1 monoclonal antibody conjugated via a cleavable linker to a high-potency topoisomerase I inhibitor. After binding EGFR on tumor cells and internalization/cleavage, it releases the TOP1 inhibitor to block DNA topoisomerase I, causing DNA damage, replication arrest, and apoptosis; the antibody may also inhibit EGFR signaling and can mediate bystander killing.
YES
DIRECT
An EGFR-targeting ADC binds EGFR on tumor cells, is internalized, and releases a topoisomerase I inhibitor payload that causes DNA damage/replication arrest leading to apoptosis; may also cause bystander killing.
An anti-EGFR antibody–drug conjugate (ADC) with a drug–antibody ratio of 8 that couples an EGFR-specific monoclonal antibody to a high-potency DNA topoisomerase I inhibitor. After binding EGFR and internalization, it releases the topo I inhibitor to cause DNA damage and apoptosis; the antibody component may also inhibit EGFR signaling.
EGFR-targeting IgG1 monoclonal antibody conjugated via a cleavable linker to a high-potency topoisomerase I inhibitor. After binding EGFR on tumor cells and internalization/cleavage, it releases the TOP1 inhibitor to block DNA topoisomerase I, causing DNA damage, replication arrest, and apoptosis; the antibody may also inhibit EGFR signaling and can mediate bystander killing.
NO
INDIRECT
HLX42 targets EGFR on the cell surface; after internalization it releases a topoisomerase I inhibitor that causes DNA damage and apoptosis. DNA topoisomerase I is the intracellular enzyme inhibited by the payload, not the antigen used for targeting, so cells aren’t killed because they express TOP1 per se (except via EGFR-mediated delivery or bystander effect).