ZiqiFeng
@ZiqiFeng_
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Graduate student at Scripps Research | Structure biology | Coronavirus
Joined July 2025
Excited to share our recent study (collaborated with @wchnicholas @SolidEvidence) of a wild cryptic lineage, NJ, detected in wastewater. Notably, it carries 39 unique substitutions on the RBD, and exhibits the highest ACE2 binding affinity and extensive antibody evasion.
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This is wild. Remember the NJ crytic lineage? I posted 18 months ago that the Spike was too divergent to predict ACE2 binding, and asked if someone else could figure it out. Some colleagues took me up on it. Guess what they found? 1/ https://t.co/0fZyAdHVjj
New Jersey Cryptic lineage update. Background: Cryptic lineages are evolutionarily advanced SARS-CoV-2 lineages detected in wastewater from an unknown source. We are fairly certain that these are derived from patients with persistent SARS-CoV-2 infections. 1/
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Viruses exploit host glycans to enter cells, yet the immune system can fight back using the same strategy. Here, we describe an antibody that neutralizes HCoV-HKU1 through sialoglycan receptor mimicry, revealing a unique mechanism of immune defense. https://t.co/m9eoIOPsTT
biorxiv.org
Entry of seasonal human coronavirus HKU1 (HCoV-HKU1) into host cells is facilitated by sequential binding to sialoglycans and transmembrane serine protease 2 (TMPRSS2) receptors. However, the...
Human coronavirus HKU1 neutralization by glycan receptor mimicry https://t.co/inD1USCOd3
#biorxiv_immuno
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Human coronavirus HKU1 neutralization by glycan receptor mimicry https://t.co/inD1USCOd3
#biorxiv_immuno
biorxiv.org
Entry of seasonal human coronavirus HKU1 (HCoV-HKU1) into host cells is facilitated by sequential binding to sialoglycans and transmembrane serine protease 2 (TMPRSS2) receptors. However, the...
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Happy to share another recent research about engineering CR3022. https://t.co/B82WbEHCzL
biorxiv.org
The epitope that monoclonal CR3022 binds to represents a promising target for broad protection against a wide range of human and zoonotic coronaviruses. We developed a powerful model to evaluate...
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Excited to share my second paper😊
Using immunoglobulin knock-in mice, Nair, Feng, Akauliya, Wilson @scrippsresearch Batista @mit et al rediversify germline & mature versions of the human anti-#SARSCoV2 spike antibody CR3022 to obtain broadened reactivity against human & bat coronaviruses https://t.co/f7fPH2Rx9H
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Happy to share my first paper🎉🍾
Structural and functional insights into the evolution of SARS-CoV-2 KP.3.1.1 spike protein
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Structural and functional insights into the evolution of SARS-CoV-2 KP.3.1.1 spike protein
cell.com
Feng et al. determine high-resolution cryo-EM structures of KP.3.1.1 and other mutant spike proteins and find that an S31 deletion introduces N30 glycosylation. They demonstrate that S31 deletion and...
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Using immunoglobulin knock-in mice, Nair, Feng, Akauliya, Wilson @scrippsresearch Batista @mit et al rediversify germline & mature versions of the human anti-#SARSCoV2 spike antibody CR3022 to obtain broadened reactivity against human & bat coronaviruses https://t.co/f7fPH2Rx9H
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Additionally, many recent SARS-CoV-2 mutations, including those in KP.3.1.1, recapitulate amino acid found in other sarbecoviruses, suggesting a trend of evolutionary reversion.
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However, the added N30 glycan contributes to immune evasion by disrupting the binding of a neutralizing antibody targeting the NTD.
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Mass spectrometry confirmed the presence of the new glycan and its impact on nearby glycoforms. These changes do not alter the overall spike conformation or its ability to bind ACE2.
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We solved the cryo-EM structures of the KP.3.1.1 spike protein and its complex with human ACE2, revealing that a deletion at S31 in the N-terminal domain leads to new glycosylation at N30 and a 180° flip of residue F32.
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My first paper is online now — a small milestone in my PhD journey. 🍾🎉 Big thanks to my advisors, Ian and Andrew, to my mentors for their guidance, and to my collaborators for their support.
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