| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ospA |
| Uniprot No | Q5SDL7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-161aa |
| 氨基酸序列 | MVAMEAMAAMEVMVAAMAATADTVASSAASATATEATVAMDTASLSLPLQLSPRSLPQSSLSATAATVATDTVVSSADTEVSDTEDSAATVSATASLSMLPQSSPRSLPQSSLSATAATVDSVTDMADTAMDTKQFISKGNEHFFAASYLCAWADQSAAGS |
| 预测分子量 | 20.2 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于ospA重组蛋白的3-4篇参考文献及其摘要概述：
1. **《Protective immunity elicited by recombinant outer surface protein A (OspA) of Borrelia burgdorferi》**
- **作者**：Simon, M.M., et al.
- **摘要**：该研究通过动物模型证明，重组OspA蛋白能诱导高水平抗体，有效预防伯氏疏螺旋体感染，为莱姆病亚单位疫苗开发奠定了基础。
2. **《A vaccine consisting of recombinant Borrelia burgdorferi outer-surface protein A against Lyme disease》**
- **作者**：Fikrig, E., et al.
- **摘要**：首次报道重组OspA疫苗的人体临床试验，结果显示疫苗安全且能显著激发中和抗体，为后续商业化疫苗(如LYMErix)提供了关键数据。
3. **《Role of adjuvant and antigen design in the efficacy of OspA-based Lyme disease vaccines》**
- **作者**：Erdile, L.F., et al.
- **摘要**：探讨不同佐剂(如铝佐剂)和OspA蛋白结构修饰对免疫应答的影响，发现脂化修饰的OspA结合特定佐剂可显著提升保护性抗体的持久性。
4. **《Recombinant OspA-based serodiagnosis of Lyme disease》**
- **作者**：Aguero-Rosenfeld, M.E., et al.
- **摘要**：开发基于重组OspA的ELISA检测方法，验证其在莱姆病早期诊断中的高敏感性和特异性，优于传统全细胞抗原检测。
这些研究涵盖了疫苗开发、免疫机制优化及诊断应用，均为OspA重组蛋白领域的里程碑工作。
The OspA (outer surface protein A) recombinant protein is a key antigen derived from *Borrelia burgdorferi*, the spirochete bacterium responsible for Lyme disease. OspA is a lipoprotein predominantly expressed on the bacterial surface during the tick vector phase and plays a critical role in the pathogen’s survival within ticks and transmission to mammalian hosts. Its genetic and structural conservation across *Borrelia* strains has made it a focal target for vaccine development and diagnostic research.
In the 1990s, recombinant OspA was the basis for the first Lyme disease vaccine (LYMErix™), which elicited antibodies in humans to block bacterial transmission during tick feeding. Although the vaccine was withdrawn due to limited demand and unsubstantiated safety concerns, OspA remains a cornerstone of ongoing vaccine research. Modern strategies include multivalent OspA-based vaccines targeting diverse *Borrelia* species and engineered OspA variants to improve immune responses.
OspA’s structure—a central α-helical domain flanked by β-strand-rich globular ends—has been extensively studied. The C-terminal region, which is highly conserved, contains epitopes crucial for protective immunity, while heterogeneity in the OspA N-terminal domain across strains complicates broad-spectrum vaccine design. Recombinant OspA production via *E. coli* expression systems allows scalable, cost-effective antigen generation for both immunological studies and diagnostic assays.
In diagnostics, recombinant OspA is used in serological tests to detect early Lyme disease, though cross-reactivity with other proteins remains a challenge. Recent advances explore OspA’s role in novel applications, such as mRNA vaccines and nanoparticle-based delivery platforms, aiming to enhance stability and immunogenicity. Ongoing research also investigates OspA’s interactions with host proteins and tick midgut components to uncover new therapeutic targets. Overall, OspA recombinant protein continues to be a vital tool in combating Lyme disease through innovative preventive and diagnostic approaches.
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