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måndag 19 oktober 2026

PubMed haku 19.10.2026: Nipah virus , rokotetta kehitellään. . Vastauksia 557. Kversetiinin etuja

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

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Discovery of Quercetin as a Potential Entry Inhibitor of Nipah Virus: A Path Toward Antiviral Therapy.
Alam MM, Rahman MM, Raj KH, Nahid AH, Saha P, Hossain A, Amaya M, Laing ED, Satter SM, Broder CC, Hossain ME, Rahman MZ.Int J Mol Sci. 2026 Sep 9;27(18):8026. doi: 10.3390/ijms27188026.PMID: 42794455 Free PMC article.
Nipah virus (NiV) is a zoonotic virus that causes severe encephalitis and respiratory disease with a mortality rate often exceeding 70%. ...The next potential candidates were evaluated using an established, BSL-2-compatible recombinant Cedar virus (rCe …

Abstract

Nipah virus (NiV) is a zoonotic virus that causes severe encephalitis and respiratory disease with a mortality rate often exceeding 70%. Currently, there are no licensed vaccines or therapeutics for NiV disease. This study aimed to identify and experimentally evaluate small-molecule inhibitors targeting the NiV-G (attachment) glycoprotein using integrated in silico and in vitro approaches. A high-throughput virtual screening of >215,000 compounds was conducted against the NiV-G glycoprotein, using docking and molecular dynamics (MD) simulations. The next potential candidates were evaluated using an established, BSL-2-compatible recombinant Cedar virus (rCedV)-based green fluorescent protein (GFP) reporter virus expressing the NiV-F (fusion) and G glycoproteins (rCedV-NiV-B-GFP). During MD simulations, quercetin demonstrated the most stable binding, maintaining a consistent RMSD (3.25 ± 0.3 Å). In vitro testing showed dose-dependent inhibition of rCedV-NiV-B-GFP infection. Although quercetin alone was less potent (IC50 = 24 µM; 95% CI: 7.6-93.6 µM) than a reference NiV-neutralizing monoclonal antibody mAb-7B7 (IC50 = 0.027 μg/mL; approximately 0.00018 μM; 95% CI: 0.0108 to 0.0735), combination with ascorbic acid enhanced neutralization (IC50 = 4.4 µM; 95% CI: 2.9-6.8 µM). Quercetin demonstrated a high Selectivity Index of >20.8. The study identifies quercetin as a promising small-molecule inhibitor of NiV cellular infection, potentially through a stable interaction with NiV-G at the ephrin-B2/B3 binding interface identified computationally. These findings highlight the importance of combining computational screening with BSL-2 cell-based bioassays to accelerate NiV countermeasure discovery.

Keywords: G glycoprotein; Nipah virus; molecular dynamics simulation; quercetin; small-molecule inhibitors; virtual screening.

The rVSV-EBOV-GP-NiV G rokotekandidaatti ("PHV02") uniikki kmeerinen virus Ebolaa ja Nipah viruksia vastaan

 Vaccine

. 2026 Oct 13:129113.
rVSV-ΔG-EBOV-GP-Nipah-G (also designated PHV02) replication-competent, recombinant vesicular stomatitis virus vaccine for prevention of Nipah virus disease: Standardized template with key considerations for a risk/benefit assessment
doi: 10.1016/j.vaccine.2026.129113. Online ahead of print.
Thomas P Monath 1, Joan Fusco 2, Emily Erbelding 3, Tracy Kemp 3, D Gray Heppner 3, Michele DeVries 3, Richard Nichols 2, Joseph D Crowell 2, Kelly Scappaticci 2, Thaddeus G Pullano 2, Heinz Feldmann 4, Friederike Feldmann 4, Emily R Wellman 5, Eileen C Farnon 6, Robert T Chen 6, Shelly Karuna 6; Brighton Collaboration Benefit-Risk Assessment of Vaccines by Technology (BRAVATO)

Free articleAbstractA recombinant vesicular stomatitis virus (rVSV) expressing the glycoprotein (GP) of Ebola virus (rVSV-EBOV GP) has been approved for preventive immunization against Ebola (Ervebo®, Merck & Co.). 

The rVSV-EBOV vector was modified to express an additional glycoprotein (G) of Nipah virus (NiV), a bat-borne henipavirus endemic/epidemic in South and Southeast Asia that causes fatal encephalitis and pneumonia. 

The rVSV-EBOV-GP-NiV G vaccine candidate ("PHV02") is a unique chimeric virus with tropism and immunological properties derived from the wild-type (wt) vesicular stomatitis virus (VSV) parent, the rVSV-EBOV-GP vector and the NiV G transgene donor. 

The EBOV GP enables fusion with the cell membrane and virus entry, whereas the NiV G protein mediates attachment to cells and serves as the antigen for stimulating NiV-specific immunity. 

This review focuses on the characteristics of the vector and vaccine candidate relevant to clinical and environmental safety, immunogenicity and efficacy. 

The Brighton Collaboration Benefit-Risk Assessment of VAccines by TechnolOgy (BRAVATO) standardized template is used to update the key characteristics and risks of the rVSV-EBOV vector (previously published [1]) and the novel PHV02 NiV vaccine candidate which is now in clinical trials. 

The template provides a rich source of information and guide to the supporting literature. While analogies of the PHV02 NiV vaccine to the backbone rVSV-EBOV vector are useful given the more extensive data available on the vector, the template emphasizes that PHV02 is a novel construct from a regulatory perspective and targets a different disease with unique characteristics and pathogenesis. 

Where similarities and parallels are drawn between nonclinical and clinical outcomes of rVSV-EBOV (vector) and PHV02 (vaccine), the reader should be cognizant of the limitations of these conclusions. The intended use of the standardized template is to provide a cohesive reference allowing vaccine developers and regulatory reviewers to understand characteristics, benefits and risks of a new vaccine candidate against NiV relevant to its future use in human populations, and to compare and contrast these characteristics to an approved vaccine constructed from the same (rVSV) vector system against a different indication (ebolavirus). The systematized template structure should facilitate utility of the paper.

Keywords: Attenuated vaccine; Brighton collaboration; Henipavirus; Immune correlate; Live; Nipah virus disease; PHV02 vaccine; Recombinant vesicular stomatitis-Ebola viral vector; Risk/benefit assessment; Vaccine safety; Vaccines.

NIPAH virus Intiassa

 https://www.is.fi/ulkomaat/art-2000011774070.html

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

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





















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 …