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Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in Aspergillus fumigatus
Hailin Zheng1,2, Huan Mei1, Xiaofang Li1,2
1Department of Medical Mycology, Institute of Dermatology, Chinese Academy of Medical Science and Peking Union Medical College, Nanjing, 210042, Jiangsu, People's Republic of China.
Abstract:
Aspergillus fumigatus is the significant causative agent in cases of invasive aspergillosis, leading to a high mortality rate in immunocompromised patients. A comprehensive understanding of its growth patterns and metabolic processes within the host is a critical prerequisite for the development of effective antifungal strategies. Lysine 2-hydroxyisobutyrylation (Khib) is a highly conserved protein posttranslational modifications (PTM) found in various organisms. In this study, we investigate the biological impact of Khib in A. fumigatus. Using a combination of antibody enrichment with the conventional LC-MS/MS method, the pattern of Khib-modification in proteins and their respective sites were analyzed in a wild type strain of A. fumigatus. Our findings revealed 3494 Khib-modified proteins with a total of 18,091 modified sites in this strain. Functional enrichment analysis indicated that these Khib-modified proteins participate in a diverse range of cellular functions, spanning various subcellular locations such as ribosome biosynthesis, protein synthesis and nucleocytoplasmic transport. Notably, when compared with other reported eukaryotes, A. fumigatus exhibited consistently higher numbers of Khib-modified proteins, suggesting the potential significance of this modification in this organism. An interesting observation is the prevalence of Khib modifications in most enzymes involved in the ergosterol synthesis pathway. The insights gathered from this study provide new avenue for studying PTM-associated mechanisms in fungal growth and offer potential implication for antifungal drug development.
Insights
Lysine 2-hydroxyisobutyrylation (Khib) is a widespread protein modification in Aspergillus fumigatus, impacting numerous proteins involved in essential cellular functions. This study identifies Khib as a potentially significant modification for fungal growth and antifungal drug development.
Area of Science:
- Mycology
- Molecular Biology
- Biochemistry
Background:
- Aspergillus fumigatus causes invasive aspergillosis with high mortality in immunocompromised individuals.
- Understanding fungal growth and metabolism is crucial for developing effective antifungal treatments.
- Lysine 2-hydroxyisobutyrylation (Khib) is a conserved protein post-translational modification (PTM) with largely unknown roles in fungi.
Purpose of the Study:
- To investigate the biological impact and prevalence of Khib in Aspergillus fumigatus.
- To identify Khib-modified proteins and their functions within A. fumigatus.
- To explore the potential of Khib as a target for antifungal drug development.
Main Methods:
- Utilized antibody enrichment combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS).
- Analyzed Khib-modified proteins and their specific modification sites in a wild-type A. fumigatus strain.
- Performed functional enrichment analysis on identified Khib-modified proteins.
Main Results:
- Identified 3,494 Khib-modified proteins and 18,091 modification sites in A. fumigatus.
- Khib-modified proteins are involved in diverse cellular functions, including ribosome biosynthesis, protein synthesis, and nucleocytoplasmic transport.
- A. fumigatus shows a higher prevalence of Khib-modified proteins compared to other eukaryotes, with notable enrichment in ergosterol synthesis pathway enzymes.
Conclusions:
- Khib is a significant PTM in A. fumigatus, affecting a wide array of cellular processes.
- The high prevalence of Khib in A. fumigatus suggests its critical role in fungal biology.
- Targeting Khib modifications, particularly in the ergosterol pathway, may offer novel strategies for antifungal drug development.
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