Frontiers in Immunology · 2023 · 22 citations · 49 references
PharmacyMedicinal ChemistryOncologyAntibody EngineeringDrug DiscoveryMolecular OncologyCancer ImmunotherapyCancer NanomedicineNanomedicineTargeted Cancer TherapyTargeted TherapyTherapeutic Antibody DevelopmentAntibody Affinity MaturationHer2 Receptor TargetingHuman Epidermal Growth Factor Receptor 2-Targeted TherapyNanobodiesNanobody DiscoveryNanobody EngineeringTherapeutic Resistance MechanismsTrastuzumab Resistance
Human epithelial growth factor receptor-2 (HER2) plays an oncogenic role in numerous tumors, including breast, gastric, and various other solid tumors. While anti-HER2 therapies are approved for the treatment of HER2-positive tumors, a necessity persists for creating novel HER2-targeted agents to resolve therapeutic resistance. Utilizing a synthetic nanobody library and affinity maturation, our study identified four anti-HER2 nanobodies that exhibited high affinity and specificity. These nanobodies recognized three distinct epitopes of HER2-ECD. Additionally, we constructed VHH-Fc and discovered that they facilitated superior internalization and showed moderate growth inhibition. Compared to the combination of trastuzumab and pertuzumab, the VHH-Fc combos or their combination with trastuzumab demonstrated greater or comparable antitumor activity in both ligand-independent and ligand-driven tumors. Most remarkably, A9B5-Fc, which targeted domain I of HER2-ECD, displayed significantly enhanced trastuzumab-synergistic antitumor efficacy compared to pertuzumab under trastuzumab-resistant conditions. Our findings offer anti-HER2 nanobodies with high affinity and non-overlapping epitope recognition. The novel nanobody-based HER2-targeted antibody, A9B5-Fc, binding to HER2-ECD I, mediates promising receptor internalization. It possesses the potential to serve as a potent synergistic partner with trastuzumab, contributing to overcoming acquired resistance.
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Pertuzumab plus Trastuzumab plus Docetaxel for Metastatic Breast Cancer
José Baselga, Javier Cortés, Sung‐Bae Kim et al. · New England Journal of Medicine · 2011 · 2.5K citations · Full text
Medicine, Oncology, Pharmacology +12
Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
Hyun‐Soo Cho, Karen Mason, Kasra X. Ramyar et al. · Nature · 2003 · 1.6K citations
Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
Matthew C. Franklin, Kendall D. Carey, F.F. Vajdos et al. · Cancer Cell · 2004 · 1.1K citations · Full text