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题    目：Biological Countermeasures Against SARS-CoV-2 Variants:From Receptor Decoys to Potent Antibodies

主讲人：Dr. Imre Kacskovics

时    间：2026年8月24日（星期一）上午10:00

地    点：第一会议室

联系人：赵要风 教授

联系方式：62731142-2003   

主讲人简介

Dr. Imre Kacskovics is Professor and Dean of the Faculty of Science at Eötvös Loránd University (ELTE) in Budapest, Hungary. He earned his Doctor of Veterinary Medicine (DVM) from the University of Veterinary Medicine in 1987 and his PhD in 1998, focusing on the characterization of swine and bovine immunoglobulin genes. He later defended his Doctoral thesis (DSc) at the Hungarian Academy of Sciences in 2013, investigating the role of FcRn in domesticated animals and enhancing immune responses by overexpressing this receptor in transgenic models.

Dr. Kacskovics joined ELTE in 2006 as an Associate Professor at the Department of Immunology and became a Full Professor and Head of the Department in 2015. Since 2019, he has served as Dean of the Faculty of Science. His research interests include molecular genetic analysis and structural-functional studies of antibodies, with significant contributions to pharmaceutical biotechnology in Hungary through patented antibody development technologies licensed globally. In 2007, he developed a patented procedure related to more efficient antibody development, which was licensed to the Japanese pharmaceutical company Kyowa Hakko Kirin in 2014 and is also utilized through his companies (ImmunoGenes Ltd. and ImmunoGenes-ABS Plc.).

报告内容:

SARS-CoV-2 evolution, particularly mutations in the spike protein, has increasingly challenged vaccine- and antibody-mediated protection through immune escape while maintaining efficient ACE2 binding. To address this, we developed two complementary biologic approaches. First, we engineered a catalytically inactive ACE2-Fc fusion protein that acts as a high-affinity soluble decoy receptor. Second, we isolated spike-specific memory B cells from vaccinated and convalescent donors and identified broadly neutralizing human monoclonal antibodies. One lead antibody showed potent cross-neutralization against multiple SARS-CoV-2 variants, including recently circulating strains. Cryo-EM analysis defined the antibody epitope and revealed binding to a highly conserved region of the spike protein. The structure further suggests that antibody binding stabilizes the spike in an RBD-down conformation, providing a potential mechanistic explanation for its broad neutralizing activity.