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源自致死性病毒的可溶性流感血凝素的皮内免疫接种可诱导高幅度和广泛的抗体反应，并在体内提供完全保护。

Intradermal Immunization of Soluble Influenza HA Derived from a Lethal Virus Induces High Magnitude and Breadth of Antibody Responses and Provides Complete Protection In Vivo.

作者信息

Raj Sneha, Vishwakarma Preeti, Saxena Shikha, Kumar Varun, Khatri Ritika, Kumar Amit, Singh Mrityunjay, Mishra Surbhi, Asthana Shailendra, Ahmed Shubbir, Samal Sweety

机构信息

Translational Health Science & Technology Institute, NCR Biotech Science Cluster, Faridabad 121001, India.

Centralized Core Research Facility (CCRF), All India Institute of Medical Sciences, New Delhi 110029, India.

出版信息

Vaccines (Basel). 2023 Mar 31;11(4):780. doi: 10.3390/vaccines11040780.

DOI:10.3390/vaccines11040780
PMID:37112692
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10141624/
Abstract

Immunogens mimicking the native-like structure of surface-exposed viral antigens are considered promising vaccine candidates. Influenza viruses are important zoonotic respiratory viruses with high pandemic potential. Recombinant soluble hemagglutinin (HA) glycoprotein-based protein subunit vaccines against Influenza have been shown to induce protective efficacy when administered intramuscularly. Here, we have expressed a recombinant soluble trimeric HA protein in Expi 293F cells and purified the protein derived from the Inf A/Guangdong-Maonan/ SWL1536/2019 virus which was found to be highly virulent in the mouse. The trimeric HA protein was found to be in the oligomeric state, highly stable, and the efficacy study in the BALB/c mouse challenge model through intradermal immunization with the prime-boost regimen conferred complete protection against a high lethal dose of homologous and mouse-adapted InfA/PR8 virus challenge. Furthermore, the immunogen induced high hemagglutinin inhibition (HI) titers and showed cross-protection against other Inf A and Inf B subtypes. The results are promising and warrant trimeric HA as a suitable vaccine candidate.

摘要

模仿表面暴露的病毒抗原天然样结构的免疫原被认为是很有前景的疫苗候选物。流感病毒是具有高大流行潜力的重要人畜共患呼吸道病毒。基于重组可溶性血凝素（HA）糖蛋白的流感蛋白亚单位疫苗经肌肉注射后已显示出诱导保护效力。在此，我们在Expi 293F细胞中表达了一种重组可溶性三聚体HA蛋白，并纯化了源自Inf A/广东-茂南/SWL1536/2019病毒的蛋白，该病毒在小鼠中具有高致病性。发现三聚体HA蛋白处于寡聚状态，高度稳定，并且通过皮内免疫采用初免-加强方案在BALB/c小鼠攻毒模型中的效力研究赋予了对高致死剂量的同源和小鼠适应的InfA/PR8病毒攻毒的完全保护。此外，该免疫原诱导了高血凝素抑制（HI）滴度，并显示出对其他Inf A和Inf B亚型的交叉保护。这些结果很有前景，证明三聚体HA是合适的疫苗候选物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/cf194d8e9ddb/vaccines-11-00780-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/420ecde18f5c/vaccines-11-00780-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/50126f7b4196/vaccines-11-00780-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/bb5d80c54f2c/vaccines-11-00780-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/cce46ec3bd33/vaccines-11-00780-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/1512f243cf64/vaccines-11-00780-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/0a6d17accca2/vaccines-11-00780-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/cf194d8e9ddb/vaccines-11-00780-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/420ecde18f5c/vaccines-11-00780-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/50126f7b4196/vaccines-11-00780-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/bb5d80c54f2c/vaccines-11-00780-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/cce46ec3bd33/vaccines-11-00780-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/1512f243cf64/vaccines-11-00780-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/0a6d17accca2/vaccines-11-00780-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e610/10141624/cf194d8e9ddb/vaccines-11-00780-g007.jpg

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