Selective capture of transcribed sequences (SCOTS) of Actinobacillus pleuropneumoniae in the chronic stage of disease reveals an HlyX-regulated autotransporter protein

Selective capture of transcribed sequences (SCOTS) of Actinobacillus pleuropneumoniae in the chronic stage of disease reveals an HlyX-regulated autotransporter protein
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DOI:
10.1016/j.vetmic.2007.03.026
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发表时间:
2007-07-20
影响因子:
3.3
通讯作者:
Gerlach, Gerald-F.
Gerlach, Gerald-F.
中科院分区:
农林科学2区
文献类型:
--
作者:
Baltes, Nina;Buettner, Falk F. R.;Gerlach, Gerald-F.

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胸膜肺炎放线杆菌是一种重要的猪呼吸道病原菌,能够在宿主组织中持续存在很长时间。在本研究中,采用选择性转录序列捕获(SCOTS)分析来鉴定A.胸膜肺炎在疾病的慢性阶段(感染后21天)。从感染的肺以及培养生长的A.胸膜肺炎,转录A.从感染的肺组织捕获胸膜肺炎病毒序列,并进行肺来源的针对培养物来源的A.胸膜肺炎cDNA。在36个被鉴定为体内表达的基因中,有29个参与运输或代谢过程。我们鉴定了一种表面相关的推定的104 kDa枯草杆菌蛋白酶样自转运蛋白丝氨酸蛋白酶,命名为AasP,其在A.胸膜肺炎该基因在所有15个A.胸膜肺炎血清型。它在感染后第7天和第21天在猪肺组织中转录。在体外厌氧条件下,其表达依赖于全局厌氧调节因子HlyX。据我们所知,这是第一个报告的自转运蛋白被全球厌氧调节。(C)2007 Elsevier B.V.保留所有权利。
Actinobacillus pleuropneumoniae, an important respiratory pathogen in swine, is able to persist in host tissues for extended periods of time. In the study presented here, selective capture of transcribed sequences (SCOTS) analysis was used to identify genes expressed by A. pleuropneumoniae in the chronic stage of the disease (21 days post infection). After isolation and reverse transcription of RNA from infected lungs as well as from culture-grown A. pleuropneumoniae, transcribed A. pleuropneumoniae sequences were captured from infected lung tissue and subjected to a subtractive hybridization procedure of lung-derived against culture-derived A. pleuropneumoniae cDNA. Twenty-nine of the thirty-six genes that were identified as in vivo-expressed are involved in transport or metabolic processes. We identified a surface-associated putative 104 kDa subtilisin-like autotransporter serine protease, designated AasP, which has not been described in A. pleuropneumoniae to date. The gene was shown to be present in all 15 A. pleuropneumoniae serotypes. It is transcribed in porcine lung tissue on days 7 and 21 post infection. Under anaerobic conditions in vitro, its expression depends on the global anaerobic regulator HlyX. To our knowledge, this is the first report of an autotransporter protein being regulated by a global anaerobic regulator. (C) 2007 Elsevier B.V. All rights reserved.