A5026862522- Glycosylation and Glycoproteins Research
- Carbohydrate Chemistry and Synthesis
- Viral gastroenteritis research and epidemiology
- SARS-CoV-2 and COVID-19 Research
- Animal Virus Infections Studies
- Genetics, Bioinformatics, and Biomedical Research
- Bacteriophages and microbial interactions
- Virus-based gene therapy research
- Machine Learning in Bioinformatics
- Monoclonal and Polyclonal Antibodies Research
National Taiwan University
2021-2025
Institute of Biological Chemistry, Academia Sinica
2021-2025
Most membrane proteins are modified by covalent addition of complex sugars through N- and O-glycosylation. Unlike proteins, glycans do not typically adopt specific secondary structures remain very mobile, shielding potentially large fractions protein surface. High glycan conformational freedom hinders complete structural elucidation glycoproteins. Computer simulations may be used to model glycosylated but require hundreds thousands computing hours on supercomputers, thus limiting routine...
Porcine epidemic diarrhea (PED) is a highly contagious swine disease caused by porcine virus (PEDV). PED causes enteric disorders with an exceptionally high fatality in neonates, bringing substantial economic losses the pork industry. The trimeric spike (S) glycoprotein of PEDV responsible for virus-host recognition, membrane fusion, and main target vaccine development antigenic analysis. atomic structures recombinant S proteins two different strains have been reported, but they reveal...
Human coronavirus 229E (HCoV-229E) is the earliest CoV found to infect humans. It binds human aminopeptidase N (hAPN) through receptor binding domain (RBD) of its spike (S) protein achieve host recognition. We present cryo-electron microscopy structure two HCoV-229E S in complex with a dimeric hAPN provide structural insights on how opens up RBD engage receptor, information that currently missing among alphacoronaviruses which belong. quantitatively profile glycosylation and deduce...
Abstract The surge of COVID-19 infection cases is spurred by emerging SARS-CoV-2 variants such as B.1.617. Here we report 38 cryo-EM structures, corresponding to the spike protein Beta (B.1.351), Gamma (P.1), Delta (B.1.617.2) and Kappa (B.1.617.1) in different functional states with without its receptor, ACE2. Mutations on N-terminal domain not only alter conformation highly antigenic supersite variant, but also remodel glycan shield deleting or adding N-glycans variants, respectively....