Ryo ShinnakasuShuhei SakakibaraHiromi YamamotoPo Hung WangSaya MoriyamaNicolas SaxChikako OnoAtsushi YamanakaYu AdachiTaishi OnoderaTakashi SatoMasaharu ShinkaiRyosuke SuzukiYoshiharu MatsuuraNoritaka HashiiYoshimasa TakahashiTakeshi InoueKazuo YamashitaTomohiro KurosakiFaculty of Tropical Medicine, Mahidol UniversityWPI Immunology Frontier Research Center, Osaka UniversityNational Institute of Infectious DiseasesResearch Institute for Microbial DiseasesRiken Research Center for Allergy and ImmunologyOsaka UniversityNational Institute of Health Sciences TokyoTokyo Shinagawa HospitalNational Institute of Infection Diseases2022-08-042022-08-042021-12-06Journal of Experimental Medicine. Vol.218, No.12 (2021)15409538002210072-s2.0-85118285956https://repository.li.mahidol.ac.th/handle/20.500.14594/77125Broadly protective vaccines against SARS-related coronaviruses that may cause future outbreaks are urgently needed. The SARS-CoV-2 spike receptor-binding domain (RBD) comprises two regions, the core-RBD and the receptor-binding motif (RBM); the former is structurally conserved between SARS-CoV-2 and SARS-CoV. Here, in order to elicit humoral responses to the more conserved core-RBD, we introduced N-linked glycans onto RBM surfaces of the SARS-CoV-2 RBD and used them as immunogens in a mouse model. We found that glycan addition elicited higher proportions of the core-RBD–specific germinal center (GC) B cells and antibody responses, thereby manifesting significant neutralizing activity for SARS-CoV, SARS-CoV-2, and the bat WIV1-CoV. These results have implications for the design of SARS-like virus vaccines.Mahidol UniversityImmunology and MicrobiologyMedicineGlycan engineering of the sars-cov-2 receptor-binding domain elicits cross-neutralizing antibodies for sars-related virusesArticleSCOPUS10.1084/JEM.20211003