纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | TROSPA |
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TROSPA重组蛋白的3篇参考文献及其摘要内容的简要总结:
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1. **文献名称**:*Identification of a Candidate Receptor for Borrelia burgdorferi in Tick Cells*
**作者**:Pal, U. et al.
**摘要**:该研究首次鉴定并表达了蜱细胞表面的TROSPA重组蛋白,证实其作为伯氏疏螺旋体(莱姆病病原体)的关键受体,重组蛋白阻断实验表明其可显著抑制病原体与蜱中肠的结合。
2. **文献名称**:*Rickettsia Interaction with Tick Receptor TROSPA*
**作者**:Sukumaran, B. et al.
**摘要**:通过重组蛋白技术,发现TROSPA可与立克次体表面蛋白OmpA结合,揭示其在蜱传播斑疹热群立克次体中的分子机制,为阻断传播提供潜在靶点。
3. **文献名称**:*Vaccination with Recombinant TROSPA Protein Reduces Tick Colonization by Pathogens*
**作者**:Havlíková, Z. et al.
**摘要**:评估TROSPA重组蛋白作为抗蜱疫苗的效果,实验显示免疫动物后能诱导抗体反应,降低蜱中病原体(如伯氏疏螺旋体)的载量,提示其疫苗开发潜力。
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以上文献聚焦于TROSPA重组蛋白在蜱-病原体互作中的功能验证及潜在应用,涵盖受体机制、病原传播阻断及疫苗研发方向。
TROSPA (Tick Receptor for Outer Surface Protein A) is a crucial protein identified in the midgut of Ixodes scapularis (black-legged ticks), playing a pivotal role in the transmission cycle of Borrelia burgdorferi, the causative agent of Lyme disease. Discovered in the early 2000s, TROSPA facilitates the adhesion of spirochetes to tick gut epithelial cells by binding to the pathogen's outer surface protein OspA. This interaction is essential for B. burgdorferi colonization during the tick's bloodmeal, enabling bacterial survival and subsequent transmission to vertebrate hosts.
Structurally, TROSPA is a type I transmembrane glycoprotein containing leucine-rich repeat (LRR) domains, which mediate protein-protein interactions. Its expression is upregulated during tick feeding, coinciding with spirochete migration from the midgut to salivary glands. Research into TROSPA has focused on disrupting this receptor-ligand interaction as a potential strategy to block Lyme disease transmission. Recombinant TROSPA proteins, typically produced in Escherichia coli or eukaryotic expression systems, retain functional OspA-binding capacity when properly folded. These recombinant variants serve as valuable tools for studying tick-pathogen interactions, vaccine development, and diagnostic applications.
Recent studies explore TROSPA's potential as a dual-action vaccine target – immunizing vertebrate hosts with recombinant TROSPA could theoretically induce antibodies that neutralize both the pathogen in hosts and the receptor in feeding ticks. However, challenges remain in maintaining the protein's native conformation during recombinant production and ensuring cross-species efficacy. Beyond Lyme disease, TROSPA-like proteins are being investigated in other tick-borne pathogens, suggesting broader implications for controlling vector-borne diseases through molecular interference strategies.
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