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特异性识别多种口蹄疫O型毒株完整衣壳的单域抗体。

Single-Domain Antibodies That Specifically Recognize Intact Capsids of Multiple Foot-and-Mouth Disease Serotype O Strains.

作者信息

Harmsen Michiel M, Gupta Nishi, Dijkstra Quillan, Water Sandra van de, Setten Marga van, Dekker Aldo

机构信息

Wageningen Bioveterinary Research, P.O. Box 65, 8200 AB Lelystad, The Netherlands.

出版信息

Vaccines (Basel). 2025 May 8;13(5):500. doi: 10.3390/vaccines13050500.

DOI:10.3390/vaccines13050500
PMID:40432111
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12116120/
Abstract

BACKGROUND/OBJECTIVES: Intact (146S) foot-and-mouth disease virus (FMDV) particles easily dissociate into 12S particles with a concomitant decreased immunogenicity. Vaccine quality control with 146S-specific single-domain antibodies (VHHs) is hampered by the high strain specificity of most 146S-specific VHHs. This study aimed to isolate 146S-specific VHHs that recognize all serotype O strains.

METHODS

Biopanning was performed with the FMDV strain O/SKR/7/2010 146S, using a secondary library of mutagenized M170F VHH that did not recognize O/SKR/7/2010 or using phage-display libraries from llamas immunized with other serotype O strains. Novel VHHs were yeast-produced and their strain-, particle-, and antigenic-site specificities were determined by ELISA.

RESULTS

M170F mutagenesis did not improve the cross-reaction with O/SKR/7/2010. However, selection from immune libraries resulted in four VHHs that exhibited high 146S specificity for all five serotype O strains analyzed. These VHHs presumably recognize all serotype O strains since the five strains analyzed represent different phylogenetic clades. They bind the same antigenic site as M170F, which was previously shown to be a conserved site in serotypes A and O, and which has an altered 3D structure when 146S dissociates into 12S particles. M916F had the lowest limit of detection, which varied from 0.7 to 5.9 ng/mL 146S particles for three serotype O strains.

CONCLUSIONS

We identified four VHHs (M907F, M910F, M912F, and M916F) that specifically bind 146S particles of probably all serotype O strains. They enable further improved FMDV vaccine quality control.

摘要

背景/目的：完整的（146S）口蹄疫病毒（FMDV）颗粒容易解离成12S颗粒，同时免疫原性降低。大多数146S特异性单域抗体（VHH）的高毒株特异性阻碍了用146S特异性VHH进行疫苗质量控制。本研究旨在分离识别所有O型毒株的146S特异性VHH。

方法

使用FMDV毒株O/SKR/7/2010 146S进行生物淘选，使用不识别O/SKR/7/2010的诱变M170F VHH二级文库，或使用用其他O型毒株免疫的美洲驼的噬菌体展示文库。新型VHH在酵母中产生，并通过ELISA测定其毒株、颗粒和抗原位点特异性。

结果

M170F诱变并未改善与O/SKR/7/2010的交叉反应。然而，从免疫文库中筛选得到了四种VHH，它们对所分析的所有五种O型毒株均表现出高146S特异性。由于所分析的五种毒株代表不同的系统发育分支，这些VHH可能识别所有O型毒株。它们与M170F结合相同的抗原位点，先前已证明该位点在A型和O型血清型中是保守位点，并且当146S解离成12S颗粒时其三维结构会发生改变。M916F的检测限最低，对于三种O型毒株，其检测限在0.7至5.9 ng/mL 146S颗粒之间。

结论

我们鉴定出四种VHH（M907F、M910F、M912F和M916F），它们特异性结合可能所有O型毒株的146S颗粒。它们有助于进一步改进FMDV疫苗质量控制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/1780c1b1329d/vaccines-13-00500-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/02d14daf5585/vaccines-13-00500-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/f8957a7ad961/vaccines-13-00500-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/297b1949a0f4/vaccines-13-00500-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/5eb5196885aa/vaccines-13-00500-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/b0ddb7476bcc/vaccines-13-00500-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/b89a7eb36f48/vaccines-13-00500-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/1780c1b1329d/vaccines-13-00500-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/02d14daf5585/vaccines-13-00500-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/f8957a7ad961/vaccines-13-00500-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/297b1949a0f4/vaccines-13-00500-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/5eb5196885aa/vaccines-13-00500-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/b0ddb7476bcc/vaccines-13-00500-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/b89a7eb36f48/vaccines-13-00500-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/608b/12116120/1780c1b1329d/vaccines-13-00500-g007.jpg

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A broadly reactive ultralong bovine antibody that can determine the integrity of foot-and-mouth disease virus capsids.一种广谱反应性的超长牛抗体，可用于检测口蹄疫病毒衣壳的完整性。
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Nat Commun. 2024 Oct 10;15(1):8774. doi: 10.1038/s41467-024-53027-5.
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A comparison of the binding sites of antibodies and single-domain antibodies.抗体和单域抗体结合位点的比较。
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