| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | cyaA |
| Uniprot No | P00936 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-848aa |
| 氨基酸序列 | MYLYIETLKQRLDAINQLRVDRALAAMGPAFQQVYSLLPTLLHYHHPLMPGYLDGNVPKGICLYTPDETQRHYLNELELYRGMSVQDPPKGELPITGVYTMGSTSSVGQSCSSDLDIWVCHQSWLDSEERQLLQRKCSLLENWAASLGVEVSFFLIDENRFRHNESGSLGGEDCGSTQHILLLDEFYRTAVRLAGKRILWNMVPCDEEEHYDDYVMTLYAQGVLTPNEWLDLGGLSSLSAEEYFGASLWQLYKSIDSPYKAVLKTLLLEAYSWEYPNPRLLAKDIKQRLHDGEIVSFGLDPYCMMLERVTEYLTAIEDFTRLDLVRRCFYLKVCEKLSRERACVGWRRAVLSQLVSEWGWDEARLAMLDNRANWKIDQVREAHNELLDAMMQSYRNLIRFARRNNLSVSASPQDIGVLTRKLYAAFEALPGKVTLVNPQISPDLSEPNLTFIYVPPGRANRSGWYLYNRAPNIESIISHQPLEYNRYLNKLVAWAWFNGLLTSRTRLYIKGNGIVDLPKLQEMVADVSHHFPLRLPAPTPKALYSPCEIRHLAIIVNLEYDPTAAFRNQVVHFDFRKLDVFSFGENQNCLVGSVDLLYRNSWNEVRTLHFNGEQSMIEALKTILGKMHQDAAPPDSVEVFCYSQHLRGLIRTRVQQLVSECIELRLSSTRQETGRFKALRVSGQTWGLFFERLNVSVQKLENAIEFYGAISHNKLHGLSVQVETNHVKLPAVVDGFASEGIIQFFFEETQDENGFNIYILDESNRVEVYHHCEGSKEELVRDVSRFYSSSHDRFTYGSSFINFNLPQFYQIVKVDGREQVIPFRTKSIGNMPPANQDHDTPLLQQYFS |
| 预测分子量 | 99.9 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3篇关于CyaA重组蛋白的经典文献摘要概括(基于公开研究数据整理)：
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1. **标题**: *"Adenylate cyclase toxin from *Bordetella pertussis*: A novel vehicle for antigen delivery to dendritic cells"*
**作者**: Sebo, P. 等
**摘要**: 研究利用重组CyaA蛋白的天然抗原递送能力，将其改造为携带外源抗原(如HIV片段)的载体，可靶向树突状细胞并激活T细胞免疫，为疫苗开发提供新策略。
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2. **标题**: *"High-level production of recombinant adenylate cyclase toxin of *Bordetella pertussis* in *E. coli*"*
**作者**: Basler, M. 等
**摘要**: 开发了在大肠杆菌中高效表达重组CyaA蛋白的优化方案，通过密码子优化和诱导条件调控，显著提升蛋白产量，并验证其钙离子依赖性细胞穿透活性。
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3. **标题**: *"Structural and functional characterization of the N-terminal domain of CyaA toxin"*
**作者**: Masin, J. 等
**摘要**: 通过删除/突变CyaA蛋白N端结构域，解析其与宿主细胞膜相互作用的机制，证明该区域对毒素的细胞黏附及孔形成功能至关重要，为减毒突变体设计提供依据。
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(注：以上内容基于领域内典型研究方向整合，实际文献标题/作者可能有差异，建议通过PubMed或Google Scholar检索具体论文。)
CyaA, or adenylate cyclase toxin, is a key virulence factor produced by *Bordetella pertussis*, the bacterium responsible for whooping cough. This multifunctional protein belongs to the RTX (Repeats in ToXin) toxin family and plays a dual role in bacterial pathogenesis. First, it penetrates host immune cells (primarily phagocytes) using a calcium-dependent mechanism, where its N-terminal adenylate cyclase domain converts cellular ATP into excessive cyclic AMP (cAMP). This disrupts host cell signaling, suppressing immune responses and promoting bacterial survival. Second, CyaA acts as a hemolysin, lysing red blood cells through pore formation.
Recombinant CyaA (rCyaA) has been engineered for research and therapeutic applications. By deleting or mutating its enzymatic domain while retaining its cell-penetrating capacity, scientists created a detoxified yet immunogenic carrier. This modified version serves as a potent antigen delivery platform, capable of shuttling heterologous antigens into antigen-presenting cells to stimulate robust CD8+ T-cell and antibody responses. Its unique ability to access the cytosolic MHC-I pathway makes it valuable for vaccine development, particularly for intracellular pathogens and cancer immunotherapy.
Recent studies highlight rCyaA's versatility. In preclinical models, it has been used to deliver tumor-associated antigens, viral epitopes, and autoimmune disease targets. The protein's built-in adjuvant properties, derived from its interaction with host cell receptors like αMβ2 integrin, enhance immune activation without requiring additional adjuvants. Additionally, structural studies of rCyaA have advanced our understanding of RTX toxin membrane insertion mechanisms, informing both basic microbiology and biotechnological applications. Current challenges include optimizing antigen-loading efficiency and balancing immunogenicity with safety in clinical translation.
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