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    • 10. 发明申请
    • Staphylococcal Phage2638A Endolysin Amidase Domain Is Lytic for Staphylococcus aureus
    • 葡萄球菌噬菌体2638A内溶素酰胺酶域是金黄色葡萄球菌的裂液
    • US20130336954A1
    • 2013-12-19
    • US13495536
    • 2012-06-13
    • David M. DonovanIgor V. Abaev
    • David M. DonovanIgor V. Abaev
    • C12N9/24C12N15/70A61P31/04A01K67/027A61K38/47C12N15/56C12N1/21
    • C12N9/80A61K38/00A61L2/16C07K14/005C12N15/52C12N2795/10322C12N2795/10332C12N2795/10333C12Y305/01028
    • Staphylococcus aureus is notorious for developing resistance to virtually all antibiotics to which it is exposed. Staphylococcal phage 2638A endolysin is a peptidoglycan hydrolase that is lytic for S. aureus when exposed externally, making it a new antimicrobial candidate. It shares a common protein organization with over 40 other staphylococcal peptidoglycan hydrolases: a CHAP endopeptidase domain, a mid-protein amidase 2 domain and a C-terminal SH3b cell wall binding domain. It is the first phage endolysin reported with a cryptic translational start site between the CHAP and amidase domains. Deletion analysis indicates that the amidase domain confers most of the lytic activity and requires the full SH3b domain for maximal activity. It is common for one domain to demonstrate dominant activity over another; however, the phage 2638A endolysin is the first to show high amidase domain activity dominant over the N-terminal CHAP domain, an important finding for targeting novel peptidoglycan bonds.
    • 金黄色葡萄球菌对于暴露于几乎所有抗生素的抗性都是臭名昭着的。 葡萄球菌噬菌体2638A细胞内溶素是一种肽聚糖水解酶,当外露时会溶解金黄色葡萄球菌,使其成为新的抗菌药物。 它与40多种其他葡萄球菌肽聚糖水解酶共享一个共同的蛋白质组织:CHAP内肽酶结构域,中蛋白酰胺酶2结构域和C末端SH3b细胞壁结合结构域。 这是第一个噬菌体内溶素与CHAP和酰胺酶结构域之间隐藏的翻译起始位点。 缺失分析表明,酰胺酶结构域赋予大部分裂解活性,并需要完整的SH3b结构域进行最大活性。 一个领域通常表现出超过另一个领域的主导地位; 然而,噬菌体2638A细胞内溶素是首先显示高N-酰基端结构域活性优于N末端CHAP结构域,这是靶向新型肽聚糖键的重要发现。