Nipah-virusta neutraloivaa bispesifistä nanovasta-aineen muodostusta (2026)

 https://pubmed.ncbi.nlm.nih.gov/?term=nipah+virus+review&sort=date

A dual-glycoprotein-targeting bispecific nanoantibody confers potent neutralization against Nipah virus.

Wang S, Zhang X, Zhang H, Rao G, Yao Y, Tian G, Gao G, Peng Y, Li W, Cao S, Chiu S, Gong R, Chen L. Virol Sin. 2026 Oct 9:S1995-820X(26)00176-8. doi: 10.1016/j.virs.2026.09.014. Online ahead of print.PMID: 42849849 Free article.

Nipah virus (NiV) is a biosafety level 4 pathogen that has consistently posed a significant threat to public health.

Abstract

Nipah virus (NiV) is a biosafety level 4 pathogen that has consistently posed a significant threat to public health. The two envelope proteins on the viral surface, the receptor-binding protein (RBP) and the fusion (F) protein, are the primary targets of neutralizing antibodies. 

However, the use of antibodies targeting a single viral antigen often leads to the emergence of resistant strains. 

Here, by panning phage display library, we obtained a C-type nanoantibody (C-Nab), G-3-1, targeting the head domain of RBP. The half-life-extended G-3-1-HLE effectively protected hamsters against authentic NiV challenge. 

Furthermore, we constructed a fusion protein, 2A1-3-8-(AP)12-G-3-1, by linking G-3-1 to the F-targeting nanobody 2A1-3-8 via a rigid (AP)12 linker.

This fusion protein exhibited improved and balanced neutralizing activity. 

In addition, the in vivo prophylactic efficacy of 2A1-3-8-(AP)12-G-3-1 was validated in a mouse model of NiV pseudovirus infection. 

Collectively, this study on a dual-envelope-protein-targeting bispecific antibody not only provides a promising antiviral candidate, but also offers an important design strategy for next-generation antibody optimization.

Keywords

Nipah virus (NiV)

Fusion protein (F)

Receptor binding protein (RBP)

Rigid linker 

Dual-glycoproteins target

Bispecific nanoantibodies

Highlights

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  G-3-1-HLE effectively protects hamsters against Nipah virus infection.
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  G-3-1 targets the head domain of Nipah virus receptor binding protein.
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  The 24-residue rigid linker, (AP)12, is optimal for linking two nanoantibodies in tandem.
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  2A1-3-8-(AP)12-G-3-1 shows superior NiV neutralization to 2A1-3-8 and G-3-1.
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  2A1-3-8-(AP)12-G-3-1 shows prophylactic efficacy against NiV pseudovirus in mice.
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Emerging respiratory infectious diseases: Clinical aspects for rapid identification and management.

Rolling T, Brehm TT, Krammer F, Addo M, Schmiedel S, Salzer H.Respiration. 2026 Oct 7:1. doi: 10.1159/res/aepag021. Online ahead of print.PMID: 42842561 Free article. Review.

We focus on zoonotic influenza A viruses, including contemporary H5N1, Middle East respiratory syndrome coronavirus (MERS-CoV), hantaviruses, Nipah virus, and inhalational bacterial threats such as anthrax, pneumonic plague, tularemia, and melioidosis. ...By integra …