unassigned: To obtain endolysin with impact(s) on gram-negative bacteria as well as gram-positive bacteria, N-acetylmuramyl L-alanine-amidase (MurNAc-LAA) from a -hosted Siphoviridae phage (SPP1 phage, Subtilis Phage Pavia 1) was exogenously expressed in .
unassigned: The sequences of genes encoding peptidoglycan hydrolases were obtained from the Virus-Host database. The sequence of MurNAc-LAA was optimized by GenScript software to generate MurNAc-LAA-MMI (LysM2) for optimal expression in . Furthermore, the structure and function of LysM2 was evaluated . The optimized gene was synthesized, subcloned in the pET28a, and expressed in BL21(DE3). The antibacterial effects of the protein on the peptidoglycan substr... More
unassigned: To obtain endolysin with impact(s) on gram-negative bacteria as well as gram-positive bacteria, N-acetylmuramyl L-alanine-amidase (MurNAc-LAA) from a -hosted Siphoviridae phage (SPP1 phage, Subtilis Phage Pavia 1) was exogenously expressed in .
unassigned: The sequences of genes encoding peptidoglycan hydrolases were obtained from the Virus-Host database. The sequence of MurNAc-LAA was optimized by GenScript software to generate MurNAc-LAA-MMI (LysM2) for optimal expression in . Furthermore, the structure and function of LysM2 was evaluated . The optimized gene was synthesized, subcloned in the pET28a, and expressed in BL21(DE3). The antibacterial effects of the protein on the peptidoglycan substrates were studied.
unassigned: , on 816 gene encoding a 33 protein was confirmed as specific SPP1 phage enzyme. The enzyme is composed of 271 amino acids, with a half-life of 10 in . analyses showed 34.2% alpha-helix in the secondary structure, hydrophobic N-terminal, and lysine-rich C-terminal, and no antigenic properties in LysM2 protein. This optimized endolysin revealed impacts against (sp) by turbidity, and an antibacterial activity against , and in agar diffusion assays.
unassigned: Taken together, our results confirmed that LysM2 is an inhibiting agent for gram-negative bacteria.
