Ehrlichia chaffeensis tandem repeat proteins and Ank200 are type 1 secretion system substrates related to the repeats-in-toxin exoprotein family.
Ehrlichia chaffeensis tandem repeat proteins and Ank200 are type 1 secretion system substrates related to the repeats-in-toxin exoprotein family.
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DOI：
10.3389/fcimb.2011.00022
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发表时间：
2011
影响因子：
5.7
通讯作者：
McBride JW
中科院分区：
文献类型：
--
作者：
Wakeel A;den Dulk-Ras A;Hooykaas PJ;McBride JW
查菲埃里希体有1型和4型分泌系统（T1 SS和T4 SS），但底物尚未确定。潜在的底物包括分泌的串联重复蛋白（TRP）47、TRP 120和TRP 32，以及锚蛋白重复蛋白Ank 200，它们参与分子宿主-病原体相互作用，包括DNA结合和蛋白质-蛋白质相互作用网络，与信号传导、转录调节、囊泡运输和凋亡相关的宿主靶标。在这项研究中，我们报告，E。在常规用于鉴定T4 SS底物的根癌农杆菌Cre重组酶报告基因测定中，查菲酵母TRP 47、TRP 32、TRP 120和Ank 200不分泌。相反，所有TRP和Ank 200蛋白由补充有溶血素分泌系统（T1 SS）的大肠杆菌分泌，并且在T1 SS突变体（ΔTolC）中分泌减少，证明这些蛋白是T1 SS底物。此外，T1 SS分泌信号在TRP和Ank 200的C-末端结构域中被鉴定，并且详细的生物信息学分析E. Chaffeensis TRP和Ank 200的特征与毒素中重复序列（RTX）家族的胞外蛋白一致，包括富含甘氨酸和谷氨酸的串联重复序列、与ATP转运蛋白的同源性、不可切割的C末端T1 SS信号、酸性pIs以及与其他T1 SS底物一致的功能。利用异源E. coli T1 SS中，本研究首次鉴定了埃里希体T1 SS的底物，支持了T1 SS和相应底物参与宿主-病原体分子相互作用的结论，这些相互作用有助于埃里希体的病理生物学。埃里希体TRP，Ank 200，和RTX外蛋白家族之间的关系的进一步调查可能会导致更好地了解T1 SS底物的重要性和特定功能的T1 SS专性细胞内细菌的病理生物学。
Ehrlichia chaffeensis has type 1 and 4 secretion systems (T1SS and T4SS), but the substrates have not been identified. Potential substrates include secreted tandem repeat protein (TRP) 47, TRP120, and TRP32, and the ankyrin repeat protein, Ank200, that are involved in molecular host–pathogen interactions including DNA binding and a network of protein–protein interactions with host targets associated with signaling, transcriptional regulation, vesicle trafficking, and apoptosis. In this study we report that E. chaffeensis TRP47, TRP32, TRP120, and Ank200 were not secreted in the Agrobacterium tumefaciens Cre recombinase reporter assay routinely used to identify T4SS substrates. In contrast, all TRPs and the Ank200 proteins were secreted by the Escherichia coli complemented with the hemolysin secretion system (T1SS), and secretion was reduced in a T1SS mutant (ΔTolC), demonstrating that these proteins are T1SS substrates. Moreover, T1SS secretion signals were identified in the C-terminal domains of the TRPs and Ank200, and a detailed bioinformatic analysis of E. chaffeensis TRPs and Ank200 revealed features consistent with those described in the repeats-in-toxins (RTX) family of exoproteins, including glycine- and aspartate-rich tandem repeats, homology with ATP-transporters, a non-cleavable C-terminal T1SS signal, acidic pIs, and functions consistent with other T1SS substrates. Using a heterologous E. coli T1SS, this investigation has identified the first Ehrlichia T1SS substrates supporting the conclusion that the T1SS and corresponding substrates are involved in molecular host–pathogen interactions that contribute to Ehrlichia pathobiology. Further investigation of the relationship between Ehrlichia TRPs, Ank200, and the RTX exoprotein family may lead to a greater understanding of the importance of T1SS substrates and specific functions of T1SS in the pathobiology of obligately intracellular bacteria.
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影响因子：
4.5
作者：
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影响因子：
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影响因子：
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作者：
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影响因子：
56.9
作者：
BEIJERSBERGEN, A;DENDULKRAS, A;HOOYKAAS, PJJ
通讯作者：
HOOYKAAS, PJJ