ArticleJournal of virology2026
ACE2-fused nanobody targeting a cryptic RBD epitope broadly neutralizes SARS-like viruses.
Article in Journal of virology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The SARS-CoV-2 (SARS2) and SARS-CoV (SARS1) viruses pose significant threats due to their high mutation rates and potential for cross-species transmission, which has rendered many antibodies ineffective. To counter potential future emergences of novel SARS-like viruses, it is imperative to develop nanobodies with broad-spectrum neutralizing capacity. Here, we employed an alternating immunization strategy in alpacas using SARS1 and SARS2 RBDs to generate cross-reactive nanobodies. Four crossing-binding nanobodies (aSR29, aSR196, aSR347, and aSR348) were identified, exhibiting high affinities for SARS1/SARS2 RBDs and Omicron subvariants. Structural analysis revealed that aSR29 targets a cryptic, highly conserved epitope at the inner base of the RBD, a region shielded from conventional antibodies by steric hindrance, efficiently neutralizing SARS1, SARS2, and multiple Variants of Concern (VOCs), including XBB.1.5 and BQ.1.1. Building on this unique binding mode, we engineered a bispecific fusion protein, aSR29-ACE2-Fc. This construct synergistically combines high-affinity RBD binding with the steric blockade of viral attachment, resulting in a 33-fold increase in neutralization potency against SARS2 and enhanced resilience against immune escape. Our findings validate an efficient strategy for eliciting broad-spectrum nanobodies and demonstrate the therapeutic potential of VHH-ACE2 fusion proteins against current and future SARS-like viruses.IMPORTANCEThe continued evolution of SARS-CoV-2 has rendered most existing antibodies ineffective, highlighting the urgent need for broad-spectrum countermeasures against current and future SARS-like viruses. Here, we developed an alternating immunization strategy to generate nanobodies that target a hidden, highly conserved region on the viral spike protein. One such nanobody, aSR29, potently neutralizes diverse variants, including XBB.1.5 and BQ.1.1. By fusing aSR29 with the viral receptor ACE2, we created a bispecific molecule that blocks viral entry through two independent mechanisms, achieving a 33-fold increase in neutralization potency. This work provides a practical and scalable strategy for pandemic preparedness, demonstrating that engineered nanobody-ACE2 fusions can serve as effective broad-spectrum therapeutics against emerging SARS-like viruses.
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