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meta-Directing Deactivators: –NO2, –CN, –CHO, –⁠CO2R, –COR, –CO2H01:13

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All meta-directing substituents are deactivating groups. These substituents withdraw electrons from the aromatic ring, making the ring less reactive toward electrophilic substitution. For example, the nitration of nitrobenzene is 100,000 times slower than that of benzene because of the deactivating effect of the nitro group. The first step in an electrophilic aromatic substitution is the addition of an electrophile to form a resonance-stabilized carbocation. The energy diagrams for...
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Updated: Feb 10, 2026

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Mapping SARS-CoV-2 Nucleocapsid Function with Nanobodies.

Jules B Reyes-Weinstein1, Timothy A Bates1, Aidan Anastas1

  • 1Department of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, OR, 97239, USA.

Biorxiv : the Preprint Server for Biology
|February 9, 2026
PubMed
Summary
This summary is machine-generated.

Alpaca-derived nanobodies targeting the SARS-CoV-2 nucleocapsid (N) protein

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Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • The SARS-CoV-2 nucleocapsid (N) protein is crucial for viral replication and immune modulation.
  • Understanding the specific functions of the N protein's domains (NTD, CTD, LINK) is limited due to its complexity.
  • The N protein's role in intracellular organization and immune evasion requires further investigation.

Purpose of the Study:

  • To develop and characterize domain-specific nanobodies (VHHs) against the SARS-CoV-2 N protein.
  • To investigate the functional roles of the N protein's individual domains using these VHHs.
  • To explore the therapeutic potential of VHHs targeting the N protein.

Main Methods:

  • Generation of twelve alpaca-derived nanobodies (VHHs) targeting N-terminal domain (NTD), C-terminal domain (CTD), and linker (LINK) regions.
  • Binding affinity characterization using ELISA and biolayer interferometry.
  • Epitope mapping via hydrogen-deuterium exchange-mass spectrometry (HDX-MS) and structural modeling.
  • In vitro and intracellular assays to assess VHHs' effect on viral infection and N protein phase separation.

Main Results:

  • Developed VHHs targeting all three domains of the SARS-CoV-2 N protein.
  • Demonstrated that intracellular VHHs inhibit SARS-CoV-2 infection.
  • Showed that VHHs disrupt N protein phase separation in vitro.
  • Confirmed that VHHs targeting individual domains independently block phase condensation and viral replication.

Conclusions:

  • Domain-specific VHHs are effective tools for dissecting the biology of the SARS-CoV-2 N protein.
  • All three domains (NTD, CTD, LINK) of the N protein are functionally important for viral replication.
  • These VHHs show significant potential for therapeutic applications against SARS-CoV-2 and other coronaviruses.