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细菌素受体鉴定的“Upp”-转。

An 'Upp'-turn in bacteriocin receptor identification.

机构信息

Teagasc Food Research Centre, Moorepark, Fermoy, Cork, Ireland; Alimentary Pharmabiotic Centre, Cork, Ireland.

出版信息

Mol Microbiol. 2014 Jun;92(6):1159-63. doi: 10.1111/mmi.12645. Epub 2014 May 19.

DOI:10.1111/mmi.12645
PMID:24811684
Abstract

Bacteriocins are gene encoded, bacterially produced antimicrobial peptides that have been the focus of considerable scientific interest but which are relatively underutilized by the food, veterinary and medical industries. One means via which the latter issue can be overcome is through a better understanding of how these peptides work or, more specifically, the identification of bacteriocin receptors and the subsequent application of such information to enhance the potency, and commercial value, of bacteriocins. For a time since the identification of lipid II and subunits of the mannose phosphotransferase system as receptors for several class I (modified) and class II (unmodified) bacteriocins, respectively, there were relatively few developments in this area. However, a number of recent studies have addressed this issue, resulting in the identification of a maltose ABC transporter and metallopeptidase as the targets for the garvicin ML (class IIc) and LsbB (class IId) bacteriocins, respectively, and, most recently, the identification of UppP as the receptor for lactococcin G and enterocin 1071 (both class IIb). In addition to these exciting discoveries, the development, and further application, of new strategies to facilitate receptor identification has the potential to lead to even further breakthroughs in bacteriocin research.

摘要

细菌素是由基因编码、细菌产生的抗菌肽,它们一直是相当多科学研究的重点,但在食品、兽医和医疗行业的应用相对较少。克服后一个问题的一种方法是通过更好地了解这些肽如何工作,或者更具体地说,识别细菌素受体,以及随后应用这些信息来提高细菌素的效力和商业价值。自脂质 II 和甘露糖磷酸转移酶系统亚基被分别鉴定为几种 I 类(修饰)和 II 类(未修饰)细菌素的受体以来,该领域的发展相对较少。然而,最近的一些研究解决了这个问题,导致鉴定出麦芽糖 ABC 转运蛋白和金属肽酶分别为 garvicin ML(IIc 类)和 LsbB(IId 类)细菌素的靶标,以及最近鉴定出 UppP 为乳球菌素 G 和肠球菌素 1071(均为 IIb 类)的受体。除了这些令人兴奋的发现外,开发和进一步应用新的策略来促进受体识别有可能为细菌素研究带来更大的突破。

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