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14.大神们，帮忙翻译一篇文献吧，急急急！
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就是这篇文献，下面有原文文件，谢谢大神们！！ Structural variations of the cell wall precursor lipid II in Gram-positive bacteria: Impact on binding and efficacy of antimicrobial peptides By Muench, Daniela; Sahl, Hans-Georg From Biochimica et Biophysica Acta, Biomembranes (2015), 1848(11_Part_B), 3062-3071. Language: English, Database: CAPLUS, DOI:10.1016/j.bbamem.2015.04.014 A review. Antimicrobial peptides (AMPs) are natural antibiotics produced by virtually all living organisms. Typically, AMPs are cationic and amphiphilic and first contacts with target microbes involve interactions with neg. charged components of the cell envelope such as lipopolysaccharide (LPS) and wall- or lipoteichoic acids (WTA, LTA). The importance of charge-mediated interactions of AMPs with the cell envelope is reflected by effective microbial resistance mechanisms which are based on redn. of the overall charge of these polymers. The anionic polymers are linked in various ways to the stress-bearing polymer of the cell envelope, the peptidoglycan, which is made of a highly conserved building block, a disaccharide-pentapeptide moiety that also contains charged residues. This structural element, in spite of its conservation throughout the bacterial world, can undergo genus- and species-specific modifications that also impact significantly on the overall charge of the cell envelope and on the binding affinity of AMPs. The modification reactions involved largely occur on the membrane-bound peptidoglycan building block, the so-called lipid II, which is a most prominent target for AMPs. In this review, we focus on modifications of lipid II and peptidoglycan and discuss their consequences for the interactions with various classes of AMPs, such as defensins, lantibiotics and glyco-(lipo)-peptide antibiotics. |
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2016-04-18 21:43:14, 936.49 K
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