Design of artilysin genes

Bioinformatics prediction and analysis were performed using the published complete genome sequence of H. pylori phage KHP30 ({"type":"entrez-nucleotide","attrs":{"text":"NC_019928.1","term_id":"431810540","term_text":"NC_019928.1"}}NC_019928.1) and 1961P ({"type":"entrez-nucleotide","attrs":{"text":"NC_019512.1","term_id":"422935762","term_text":"NC_019512.1"}}NC_019512.1) (Lehours et al. 2011; Luo et al. 2012; Uchiyama et al. 2012, 2013; Abdel-Haliem and Askora 2013; Takeuchi et al. 2018). Preliminary annotations and reports of H. pylori phage endolysin and holin were used in combination with the NCBI BLAST program (e-values ≤ 0.01 were considered credible); the smallest item in the credible range was subjected to the next round of BLAST. This was repeated until no obvious homologues appeared, and possible enzymatic functions were identified using the annotated H. pylori phage endolysin. The (ExPASy) Protparam software was used to analyze basic biochemical properties (e.g., amino acid length, molecular weight, isoelectric point, charge number, and hydrophilicity). Signal P3.0 software was used to analyze N-terminal amino acid sequences to determine whether they contained signal peptides. The SWISS-MODEL automatic matching method was used to predict and compare tertiary structures, using all default parameters. The above analysis and comparison were expected to identify multiple H. pylori bacteriophage endolysin and holin sequences, including Holin A, Holin B, Endolysin A and Endolysin B (see Additional file 1: Table S1). In addition, during the early stages of this study, extensive literature review and data analysis revealed several transmembrane peptides with different physical and chemical properties. Their sequences or optimized sequences (see Additional file 1: Table S2) were connected to H. pylori phage endolysin and holin using a linker (GAGA), thereby producing artilysin genes (see Additional file 1: File S1).