ArticlePLoS pathogens2022
Quantitative regulation of the thermal stability of enveloped virus vaccines by surface charge engineering to prevent the self-aggregation of attachment glycoproteins.
Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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Who cites it
10 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.
- Insights into the multifunctionality of viral glycoproteins F and HN in the lifecycle and pathogenesis of Newcastle disease virus: a systematic review.Veterinary research · 2025Pooled it
- Nondestructive tracking of viral infections by viral protein-initiated fluorescent sensors.Journal of virology · 2026Article
- Development and Characterization of a Thermostable Liquid Formulation of Live Newcastle Disease Vaccine.Veterinary sciences · 2026Article
- The landscape of gene mutations in a cohort of 3353 Han Chinese children with nonsyndromic hearing loss.EBioMedicine · 2026Article
- Article
- Residue 365 in Hemagglutinin-Neuraminidase Is a Key Thermostable Determinant of Genotype VI.2.1.1.2.2 Newcastle Disease Virus.Viruses · 2025Article
- Entry of Newcastle disease virus into host cells: an interplay among viral and host factors.Archives of virology · 2024Review
- Thermostable vacuum foam dried Newcastle disease vaccine: Process optimization and pilot-scale study.Applied microbiology and biotechnology · 2024Article
- C-terminal truncation of the hemagglutinin-neuraminidase (HN) protein enhances the virulence and immunogenicity of Newcastle disease virus (NDV) vaccine strain V4.Archives of virology · 2023Article
- Article
Corrections and comments
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Authors and funding
20 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The development of thermostable vaccines can relieve the bottleneck of existing vaccines caused by thermal instability and subsequent poor efficacy, which is one of the predominant reasons for the millions of deaths caused by vaccine-preventable diseases. Research into the mechanism of viral thermostability may provide strategies for developing thermostable vaccines. Using Newcastle disease virus (NDV) as model, we identified the negative surface charge of attachment glycoprotein as a novel determinant of viral thermostability. It prevented the temperature-induced aggregation of glycoprotein and subsequent detachment from virion surface. Then structural stability of virion surface was improved and virus could bind to and infect cells efficiently after heat-treatment. Employing the approach of surface charge engineering, thermal stability of NDV and influenza A virus (IAV) vaccines was successfully improved. The increase in the level of vaccine thermal stability was determined by the value-added in the negative surface charge of the attachment glycoprotein. The engineered live and inactivated vaccines could be used efficiently after storage at 37°C for at least 10 and 60 days, respectively. Thus, our results revealed a novel surface-charge-mediated link between HN protein and NDV thermostability, which could be used to design thermal stable NDV and IAV vaccines rationally.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.