纯度 | >90%SDS-PAGE. |
种属 | Shigella flexneri |
靶点 | mxiH |
Uniprot No | P0A223 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-83aa |
氨基酸序列 | MSVTVPNDDWTLSSLSETFDDGTQTLQGELTLALDKLAKNPSNPQLLAEYQSKLSEYTLYRNAQSNTVKVIKDVDAAIIQNFR |
预测分子量 | 16.7 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mxiH重组蛋白的3篇参考文献,涵盖结构、功能及应用研究:
1. **文献名称**:Structural characterization of the type III secretion needle protein MxiH from *Shigella flexneri*
**作者**:Deane, J.E., et al.
**摘要**:通过核磁共振和X射线晶体学解析了重组MxiH蛋白的原子结构,发现其形成螺旋纤维结构,并提出其在病原菌III型分泌系统(T3SS)针状体组装及效应蛋白分泌中的关键作用。
2. **文献名称**:Functional analysis of recombinant MxiH in the assembly of the *Shigella* type III secretion apparatus
**作者**:Blocker, A., et al.
**摘要**:研究重组MxiH蛋白在T3SS针状体组装中的功能,通过点突变实验证明其C端疏水区对针状体多聚化及效应蛋白转运至关重要,缺失突变体导致分泌功能丧失。
3. **文献名称**:Recombinant MxiH as a potential subunit vaccine against *Shigella* infection
**作者**:Martinez-Becerra, F.J., et al.
**摘要**:评估重组MxiH蛋白作为疫苗的潜力,动物实验显示其可诱导特异性抗体反应并显著提高小鼠对志贺氏菌攻击的存活率,提示其在亚单位疫苗开发中的应用前景。
(注:上述文献信息为示例性概括,实际检索时需通过PubMed或Google Scholar核对准确标题及作者。)
The mxiH protein is a key structural component of the type III secretion system (T3SS) in Gram-negative bacteria, particularly in pathogens such as *Shigella* spp. and some strains of *Escherichia coli*. The T3SS is a syringe-like molecular apparatus that enables these bacteria to inject effector proteins directly into host cells, facilitating invasion, immune evasion, and intracellular survival. MxiH, a conserved homolog of the *Salmonella* PrgI and *Yersinia* YscF proteins, forms the major subunit of the T3SS needle. This ~9 kDa protein polymerizes into a helical filament that extends from the bacterial surface, serving as a conduit for effector translocation. Its structural flexibility and dynamic assembly are critical for sensing host contact and regulating effector delivery.
Recombinant mxiH protein is produced through heterologous expression systems (e.g., *E. coli*) for functional and structural studies. Researchers utilize it to investigate needle assembly mechanics, host-pathogen interactions, and immune responses. Structural analyses, including NMR and cryo-EM, have revealed its α-helical core and conserved residues essential for oligomerization. Notably, mxiH's immunogenic properties make it a potential target for vaccines or diagnostics against shigellosis, a major cause of dysentery. Challenges in working with recombinant mxiH include maintaining solubility and native conformation due to its intrinsic aggregation propensity. Studies leveraging this protein have advanced antimicrobial strategies aimed at disrupting T3SS function, offering alternatives to traditional antibiotics in an era of rising multidrug resistance.
×