Hatton Natasha E, Wilson Laurence G, Baumann Christoph G, Fascione Martin A
Department of Chemistry, University of York York YO10 5DD UK
School of Engineering, Physics and Technology, University of York York YO10 5DD UK.
RSC Adv. 2024 Sep 13;14(40):29106-29112. doi: 10.1039/d4ra04774e. eCollection 2024 Sep 12.
Colicins are antimicrobial proteins produced by certain strains of that function as offensive weapons against closely-related competitor strains. Their bactericidal properties and narrow bacterial targeting range has made them of therapeutic interest. Furthermore, the applications of engineered non-bactericidal colicins are of interest as a cell surface-directed protein anchor for decorating with biomolecules. We previously demonstrated that an engineered non-bacteriocidal colicin E9 could be used to label bacterial cells with multiple biomolecules including glycans. Herein we extend our approach to colicin Ia, constructing mannose-presenting colicin la neoglycoproteins, through N-terminal organocatalyst-mediated protein aldol ligation (OPAL), or maleimide ligation targeting an internal cysteine. This work further highlights the potential utility of engineered colicins for non-genetic glyco-engineering of the cell surface.
大肠杆菌素是由某些大肠杆菌菌株产生的抗菌蛋白，可作为对抗密切相关竞争菌株的攻击性武器。它们的杀菌特性和狭窄的细菌靶向范围使其具有治疗价值。此外，工程化的非杀菌性大肠杆菌素作为一种用于用生物分子修饰细胞表面的细胞表面定向蛋白锚定物也备受关注。我们之前证明，一种工程化的非杀菌性大肠杆菌素E9可用于用包括聚糖在内的多种生物分子标记细菌细胞。在此，我们将方法扩展至大肠杆菌素Ia，通过N端有机催化剂介导的蛋白质醛醇连接（OPAL）或靶向内部半胱氨酸的马来酰亚胺连接，构建呈现甘露糖的大肠杆菌素Ia新糖蛋白。这项工作进一步突出了工程化大肠杆菌素在细菌细胞表面非遗传糖基工程中的潜在应用价值。
