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优化重组抗原 P29 中的绵羊 B 细胞表位用于疫苗开发。

Optimizing sheep B-cell epitopes in recombinant antigen P29 for vaccine development.

机构信息

Center of Scientific Technology, Ningxia Medical University, Yinchuan, China.

Ningxia Key Laboratory of Prevention and Treatment of Common Infectious Diseases, Ningxia Medical University, Yinchuan, China.

出版信息

Front Immunol. 2024 Aug 14;15:1451538. doi: 10.3389/fimmu.2024.1451538. eCollection 2024.

DOI:10.3389/fimmu.2024.1451538
PMID:39206186
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11349700/
Abstract

BACKGROUND

is a widespread zoonotic parasitic disease, significantly impacting human health and livestock development; however, no vaccine is currently available for humans. Our preliminary studies indicate that recombinant antigen P29 (rEg.P29) is a promising candidate for vaccine.

METHODS

Sheep were immunized with rEg.P29, and venous blood was collected at various time points. Serum was isolated, and the presence of specific antibodies was detected using ELISA. We designed and synthesized a total of 45 B cell monopeptides covering rEg.P29 using the overlap method. ELISA was employed to assess the serum antibodies of the immunized sheep for recognition of these overlapping peptides, leading to the preliminary identification of B cell epitopes. Utilizing these identified epitopes, new single peptides were designed, synthesized, and used to optimize and confirm B-cell epitopes.

RESULTS

rEg.P29 effectively induces a sustained antibody response in sheep, particularly characterized by high and stable levels of IgG. Eight B-cell epitopes of were identified, which were mainly distributed in three regions of rEg.P29. Finally, three B cell epitopes were identified and optimized: rEg.P29, rEg.P29, and rEg.P29. These optimized epitopes were well recognized by antibodies in sheep and mice, and the efficacy of these three epitopes significantly increased when they were linked in tandem.

CONCLUSION

Three B-cell epitopes were identified and optimized, and the efficacy of these epitopes was significantly enhanced by tandem connection, which indicated the feasibility of tandem peptide vaccine research. This laid a solid foundation for the development of epitope peptide vaccine for .

摘要

背景

旋毛虫病是一种广泛存在的人畜共患寄生虫病,严重影响人类健康和畜牧业发展;然而,目前人类尚无可用的疫苗。我们的初步研究表明,重组抗原 P29(rEg.P29)是一种有前途的疫苗候选物。

方法

用 rEg.P29 免疫绵羊,在不同时间点采集静脉血。分离血清,用 ELISA 检测特异性抗体的存在。我们使用重叠法设计并合成了总共 45 个覆盖 rEg.P29 的 B 细胞单肽。用 ELISA 评估免疫绵羊的血清抗体对这些重叠肽的识别情况,从而初步鉴定 B 细胞表位。利用这些鉴定出的表位,设计、合成了新的单肽,并用于优化和确认 B 细胞表位。

结果

rEg.P29 能有效诱导绵羊产生持续的抗体应答,特别是 IgG 水平高且稳定。鉴定出 8 个 B 细胞表位,主要分布在 rEg.P29 的三个区域。最后,鉴定并优化了三个 B 细胞表位:rEg.P29、rEg.P29 和 rEg.P29。这些优化后的表位在绵羊和小鼠的抗体中得到了很好的识别,当它们串联时,这些三个表位的功效显著增加。

结论

鉴定并优化了三个 B 细胞表位,串联连接显著增强了这些表位的功效,这表明串联肽疫苗研究的可行性。这为旋毛虫病的表位肽疫苗的开发奠定了坚实的基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/1a3d69295b36/fimmu-15-1451538-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/f5f63485205d/fimmu-15-1451538-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/c9979f902e92/fimmu-15-1451538-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/ee575403a92f/fimmu-15-1451538-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/5b21b1e157a1/fimmu-15-1451538-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/89054fe15815/fimmu-15-1451538-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/39e8fb8e0af3/fimmu-15-1451538-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/1a3d69295b36/fimmu-15-1451538-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/f5f63485205d/fimmu-15-1451538-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/c9979f902e92/fimmu-15-1451538-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/ee575403a92f/fimmu-15-1451538-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/5b21b1e157a1/fimmu-15-1451538-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/89054fe15815/fimmu-15-1451538-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/39e8fb8e0af3/fimmu-15-1451538-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1498/11349700/1a3d69295b36/fimmu-15-1451538-g007.jpg

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