The lysine acetylome of the nematocidal bacterium Bacillus nematocida and impact of nematode on the acetylome

Bacillus nematocida B16 (B16) is a pathogenic bacterium that is nematotoxic to plant-parasitic nematodes. In this study, we performed a quantitative lysine acetylome analysis on B16 to understand the potential roles of protein lysine acetylation on this host-pathogen interaction. Altogether, we identified 529 acetylation sites in 349 proteins, quantified 411 sites in 288 proteins, determined that the acetylation levels of 18 sites were up-regulated and those of 19 sites were down-regulated during pathogenesis. The acetylated proteins mainly participated in metabolic processes, protein synthesis, and cell wall/membrane biogenesis. Moreover, these proteins are involved in more than twenty KEGG pathways. Eight peptide motifs of acetylated proteins were identified, five of which have been thus far found only in the B16 acetylome. Twenty-two acetylated proteins were found to be involved in the synthesis of nematode attractants, and two were found to be involved in the secretion of virulence factors. In addition, the acetylation levels of ten lysine sites were regulated significantly differently in the presence of nematodes. Our results reveal that lysine acetylation may play roles in regulating B16-nematode interaction. SIGNIFICANCE: B. nematocida B16 is a bio-control bacterium against nematodes. It lures nematodes to their death by a Trojan horse mechanism. But there is little understanding about the regulation of this "Trojan horse" like pathogenesis. Lysine acetylation was reported to regulate diverse cellular processes. Our results revealed that lysine acetylation played indeed roles in regulating the B16-nematodes interaction. Our data laid a foundation for studying the molecule mechanism of lysine acetylation in regulating this host-pathogen interaction.