Abstract
AbstractGiardia lamblia (G. lamblia) is the cause of giardiasis, a common infection that affects the general population of the world. Despite the constant possibility of damage because of their own metabolism, G. lamblia has survived and evolved to adapt to various environments. However, research on energy-metabolism conversion in G. lamblia is limited. This study aimed to reveal the dynamic metabolism conversion mechanism in G. lamblia under sugar starvation by detecting global lysine acetylation (Kac) and 2-hydroxyisobutyrylation (Khib) sites combined with quantitative proteome analyses. A total of 2999 acetylation sites on 956 proteins and 8877 2-hydroxyisobutyryl sites on 1546 proteins were quantified under sugar starvation. Integrated Kac and Khib data revealed that modified proteins were associated with arginine biosynthesis, glycolysis/gluconeogenesis, and alanine, aspartate, and glutamate metabolisms. These findings suggest that Kac and Khib were ubiquitous and provide deep insight into the metabolism conversion mechanism in G. lamblia under sugar starvation. Overall, these results can help delineate the biology of G. lamblia infections and reveal the evolutionary rule from prokaryote to eukaryote.
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