Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors
Lei Guo,
Yan Liang,
Heng Li,
Huiwen Zheng,
Zening Yang,
Yanli Chen,
Xin Zhao,
Jing Li,
Binxiang Li,
Haijing Shi,
Ming Sun,
Longding Liu
Affiliations
Lei Guo
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China; Kunming Key Laboratory of Children Infection and Immunity, Yunnan Key Laboratory of Children's Major Disease Research, Yunnan Medical Center for Pediatric Diseases, Yunnan Institute of Pediatrics, Kunming Children's Hospital, Kunming, China
Yan Liang
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Heng Li
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Huiwen Zheng
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Zening Yang
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Yanli Chen
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Xin Zhao
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Jing Li
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Binxiang Li
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Haijing Shi
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Ming Sun
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China
Longding Liu
Institute of Medical Biology, Chinese Academy of Medical Science and Peking Union Medical College, Beijing, China; Corresponding author
Summary: Glycosylation of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein mediates viral entry and immune escape. While glycan site is determined by viral genetic code, glycosylation is completely dependent on host cell post-translational modification. Here, by producing SARS-CoV-2 virions from various host cell lines, viruses of different origins with diverse spike protein glycan patterns were revealed. Binding affinities to C-type lectin receptors (CLRs) DC&L-SIGN differed in the different glycan pattern virions. Although none of the CLRs supported viral productive infection, viral trans&cis-infection mediated by the CLRs were substantially changed among the different virions. Specifically, trans&cis-infection of virions with a high-mannose structure (Man5GlcNAc2) at the N1098 glycan site of the spike postfusion trimer were markedly enhanced. Considering L-SIGN co-expression with ACE2 on respiratory tract cells, our work underlines viral epigenetic glycosylation in authentic viral infection and highlights the attachment co-receptor role of DC&L-SIGN in SARS-CoV-2 infection and prevention.
