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A viral protein antibiotic inhibits lipid II flippase activity.
Nature Microbiology ( IF 20.5 ) Pub Date : 2017-Nov-01 , DOI: 10.1038/s41564-017-0023-4
Karthik R. Chamakura , Lok-To Sham , Rebecca M. Davis , Lorna Min , Hongbaek Cho , Natividad Ruiz , Thomas G. Bernhardt , Ry Young

For bacteriophage infections, the cell walls of bacteria, consisting of a single highly polymeric molecule of peptidoglycan (PG), pose a major problem for the release of progeny virions. Phage lysis proteins that overcome this barrier can point the way to new antibacterial strategies 1 , especially small lytic single-stranded DNA (the microviruses) and RNA phages (the leviviruses) that effect host lysis using a single non-enzymatic protein 2 . Previously, the A2 protein of levivirus Qβ and the E protein of the microvirus ϕX174 were shown to be 'protein antibiotics' that inhibit the MurA and MraY steps of the PG synthesis pathway 2-4 . Here, we investigated the mechanism of action of an unrelated lysis protein, LysM, of the Escherichia coli levivirus M 5 . We show that LysM inhibits the translocation of the final lipid-linked PG precursor called lipid II across the cytoplasmic membrane by interfering with the activity of MurJ. The finding that LysM inhibits a distinct step in the PG synthesis pathway from the A2 and E proteins indicates that small phages, particularly the single-stranded RNA (ssRNA) leviviruses, have a previously unappreciated capacity for evolving novel inhibitors of PG biogenesis despite their limited coding potential.

中文翻译:

病毒蛋白抗生素抑制脂质II脂酶的活性。

对于噬菌体感染,由单个高度聚合的肽聚糖(PG)分子组成的细菌细胞壁是释放子代病毒体的主要问题。克服这一障碍的噬菌体裂解蛋白可以为新的抗菌策略指明道路1,特别是小的裂解单链DNA(微病毒)和RNA噬菌体(左旋病毒),它们会使用单个非酶蛋白2进行宿主裂解。以前,鼠病毒Qβ的A 2蛋白和微小病毒ϕX174的E蛋白被证明是“蛋白抗生素”,可以抑制PG合成途径2-4的MurA和MraY步骤。在这里,我们研究了不相关的裂解蛋白Lys M的作用机理。,大肠杆菌的左旋病毒M 5。我们表明Lys M通过干扰MurJ的活性抑制了最终的脂质连接的PG前体,称为脂质II,跨细胞质膜的转运。Lys M抑制了A 2和E蛋白在PG合成途径中一个明显步骤的发现表明,小噬菌体,特别是单链RNA(ssRNA)左旋病毒,尽管具有进化出的新型PG生物发生抑制剂的能力,但以前却没有得到认可。它们有限的编码潜力。
更新日期:2017-09-11
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