VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83.
VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83.
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DOI：
10.1099/mic.0.29146-0
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发表时间：
2006-11
期刊：
影响因子：
1.5
通讯作者：
E. Vanterpool;F. Roy;W. Zhan;S. Sheets;L. Sangberg;H. Fletcher
中科院分区：
文献类型：
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作者：
E. Vanterpool;F. Roy;W. Zhan;S. Sheets;L. Sangberg;H. Fletcher
作者之前已经表明，vimA基因，这是bcp-recA-vimA操纵子的一部分，在牙龈卟啉单胞菌蛋白酶激活中起着重要作用。牙龈菌蛋白酶RgpB酶原在vimA缺陷型突变体牙龈卟啉单胞菌FLL 92中分泌。提出的一个重要问题是，vimA基因产物是否可以直接与蛋白酶相互作用以激活蛋白酶或调节负责蛋白酶激活的途径。为了进一步研究VimA依赖性蛋白酶活化的机制，进一步表征了vimA基因产物。纯化了与预测的VimA蛋白大小一致的39 kDa蛋白。在蛋白质-蛋白质相互作用研究中，显示VimA蛋白与牙龈卟啉菌蛋白酶RgpA、RgpB和Kgp相互作用。来自用牙龈卟啉单胞菌免疫的小鼠的免疫血清与纯化的VimA蛋白免疫反应。总之，这些数据表明VimA与牙龈卟啉菌蛋白酶的相互作用，并进一步证实了这种蛋白质在其调节或成熟中的作用。
The authors have shown previously that the vimA gene, which is part of the bcp-recA-vimA operon, plays an important role in protease activation in Porphyromonas gingivalis. The gingipain RgpB proenzyme is secreted in the vimA-defective mutant P. gingivalis FLL92. An important question that is raised is whether the vimA gene product could directly interact with the proteases for their activation or regulate a pathway responsible for protease activation. To further study the mechanism(s) of VimA-dependent protease activation, the vimA gene product was further characterized. A 39 kDa protein consistent with the size of the predicted VimA protein was purified. In protein-protein interaction studies, the VimA protein was shown to interact with gingipains RgpA, RgpB and Kgp. Immune sera from mice immunized with P. gingivalis immunoreacted with the purified VimA protein. Taken together, these data suggest an interaction of VimA with the gingipains and further confirm the role of this protein in their regulation or maturation.