Proteolysis of BB0323 results in two polypeptides that impact physiologic and infectious phenotypes in Borrelia burgdorferi.
Proteolysis of BB0323 results in two polypeptides that impact physiologic and infectious phenotypes in Borrelia burgdorferi.
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DOI：
10.1111/mmi.12202
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发表时间：
2013-05
影响因子：
3.6
通讯作者：
Pal U
中科院分区：
文献类型：
--
作者：
Kariu T;Yang X;Marks CB;Zhang X;Pal U
伯氏疏螺旋体基因产物BB 0323是细胞分裂和病原体体内持久性所必需的。在这里，我们表明BB 0323在全球流行的传染性菌株中是保守的，即使在细胞分裂的早期阶段也支持螺旋体的正常生长和形态。我们证明，天然BB 0323在C-末端，在前202个N-末端氨基酸后的一个位点进行蛋白水解加工。我们进一步鉴定了B中的周质BB 0323结合蛋白。burgdorferi，注释为BB 0104，具有丝氨酸蛋白酶活性，负责BB 0323的初级切割以产生离散的N-和C-末端多肽。这两种BB 0323多肽彼此相互作用，并且单独或作为复合物，与螺旋体生物学和感染性中的多种功能相关。虽然N-末端BB 0323足以支持细胞分裂，但C-末端LysM结构域对于该过程是不稳定的，尽管其具有结合B的能力。伯氏肽聚糖然而，LysM结构域或精确加工的BB 0323产物对于哺乳动物感染是必需的。由于BB 0323是对B至关重要的膜蛋白。通过研究伯氏螺旋体在体内的存活情况，探索其功能可能会提出中断感染的新方法，同时增强我们对复杂的螺旋体分裂过程的理解。
Borrelia burgdorferi gene product BB0323 is required for cell fission and pathogen persistence in vivo. Here, we show that BB0323, which is conserved amongst globally prevalent infectious strains, supports normal spirochete growth and morphology even at early phases of cell division. We demonstrate that native BB0323 undergoes proteolytic processing at the C-terminus, at a site after the first 202 N-terminal amino acids. We further identified a periplasmic BB0323-binding protein in B. burgdorferi, annotated as BB0104, having serine protease activity responsible for the primary cleavage of BB0323 to produce discrete N- and C-terminal polypeptides. These two BB0323 polypeptides interact with each other, and either individually or as a complex, are associated with multiple functions in spirochete biology and infectivity. While N-terminal BB0323 is adequate to support cell fission, the C-terminal LysM domain is dispensable for this process, despite its ability to bind B. burgdorferi peptidoglycan. However, the LysM domain or the precisely processed BB0323 product is essential for mammalian infection. As BB0323 is a membrane protein crucial for B. burgdorferi survival in vivo, exploring its function may suggest novel ways to interrupt infection while enhancing our understanding of the intricate spirochete fission process.
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影响因子：
3.2
作者：
Casjens, Sherwood R.;Mongodin, Emmanuel F.;Schutzer, Steve E.
通讯作者：
Schutzer, Steve E.
影响因子：
3.1
作者：
Kung F;Anguita J;Pal U
通讯作者：
Pal U
影响因子：
3.2
作者：
Llamas, MA;Ramos, JL;Rodríguez-Herva, JJ
通讯作者：
Rodríguez-Herva, JJ
影响因子：
3.2
作者：
PASTER, BJ;DEWHIRST, FE;WOESE, CR
通讯作者：
WOESE, CR
DOI：
10.1073/pnas.200221797
发表时间：
2000-09-26
影响因子：
11.1
作者：
Motaleb, MA;Corum, L;Charon, NW
通讯作者：
Charon, NW