Involvement of three meningococcal surface-exposed proteins, the heparin-binding protein NhbA, the α-peptide of IgA protease and the autotransporter protease NalP, in initiation of biofilm formation
Involvement of three meningococcal surface-exposed proteins, the heparin-binding protein NhbA, the α-peptide of IgA protease and the autotransporter protease NalP, in initiation of biofilm formation
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DOI：
10.1111/mmi.12097
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发表时间：
2013-01-01
影响因子：
3.6
通讯作者：
Tommassen, Jan
中科院分区：
文献类型：
--
作者：
Arenas, Jesus;Nijland, Reindert;Tommassen, Jan
脑膜炎奈瑟菌是人类鼻咽粘膜的常见且通常无害的居民，在罕见情况下，其可穿过上皮屏障并引起脑膜炎和败血症。生物膜的形成有利于宿主的定殖和随后的载体状态。脑膜炎球菌菌株的生物膜形成有两种不同的策略，依赖于或不依赖于细胞外DNA（eDNA）。在这里，我们证明了自转运蛋白酶NalP，其表达是时相可变的，影响了N.脑膜炎在静态和流动条件下，NalP的影响被发现在生物膜的形成，并依赖于其蛋白酶活性。肝素结合抗原NhbA和伊加蛋白酶的α-肽的裂解导致带正电荷的多肽从细胞表面释放，这是NalP表达时生物膜形成减少的原因。NhbA和伊加蛋白酶的α-肽都显示出结合DNA。我们的结论是，NHbA和伊加蛋白酶的a-肽有牵连的生物膜的形成，通过结合eDNA和NalP是一个重要的调节器，通过这些表面暴露的蛋白质的蛋白水解，这一过程。
Neisseria meningitidis is a common and usually harmless inhabitant of the mucosa of the human nasopharynx, which, in rare cases, can cross the epithelial barrier and cause meningitis and sepsis. Biofilm formation favours the colonization of the host and the subsequent carrier state. Two different strategies of biofilm formation, either dependent or independent on extracellular DNA (eDNA), have been described for meningococcal strains. Here, we demonstrate that the autotransporter protease NalP, the expression of which is phase variable, affects eDNA-dependent biofilm formation in N. meningitidis. The effect of NalP was found in biofilm formation under static and flow conditions and was dependent on its protease activity. Cleavage of the heparin-binding antigen NhbA and the a-peptide of IgA protease, resulting in the release of positively charged polypeptides from the cell surface, was responsible for the reduction in biofilm formation when NalP is expressed. Both NhbA and the a-peptide of IgA protease were shown to bind DNA. We conclude that NhbA and the a-peptide of IgA protease are implicated in biofilm formation by binding eDNA and that NalP is an important regulator of this process through the proteolysis of these surface-exposed proteins.