Phylogenomic analysis of non-ribosomal peptide synthetases in the genus Aspergillus
Abstract
Fungi from the genus Aspergillus are important saprophytes and opportunistic human fungal pathogens that contribute in these and other diverse ways to human well-being. Part of their impact on human well-being stems from the production of small molecular weight secondary metabolites, which may contribute to the ability of these fungi to cause invasive fungal infections and allergic diseases. In this study, we identified one group of enzymes responsible for secondary metabolite production in five Aspergillus species, the non-ribosomal peptide synthetases (NRPS). Hidden Markov models were used to search the genome databases of A. fumigatus, A. flavus, A. terreus, A. nidulans, and A. oryzae for domains conserved in NRPS proteins. A genealogy of adenylation domains was utilized to identify orthologous and unique NRPS among the Aspergillus species examined, as well as gain an understanding of the potential evolution of Aspergillus NRPS. mRNA abundance of the 14 NRPS identified in the A. fumigatus genome was analyzed using real-time reverse transcriptase PCR in different environmental conditions to gain a preliminary understanding of the possible functions of the NRPSs' peptide products. Our results suggest that Aspergillus species contain conserved and unique NRPS genes with a complex evolutionary history. This result suggests that the genus Aspergillus produces a substantial diversity of non-ribosomally synthesized peptides. Further analysis of these genes and their peptide products may identify important roles for secondary metabolites produced by NRPS in Aspergillus physiology, ecology, and fungal pathogenicity.
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Besides srbA itself, the gene with the highest fold difference in expression in SDW1 is a non-ribosomal peptide synthetase, AFUA_1g10380 (NRPS1 or pes1).
“Interestingly, besides srbA itself, the gene with the highest fold difference in expression in SDW1 is a non-ribosomal peptide synthetase, AFUA_1g10380 (NRPS1 or pes1) [43],[44].”
From A Sterol-Regulatory Element Binding Protein Is Required for Cell Polarity, Hypoxia Adaptation, Azole Drug Resistance, and Virulence in Aspergillus fumigatus (2008) · cites this paper as [43]
NRPS1 (or pes1) had the highest change in expression between wild type and the SrbA null mutant.
“For example, a non-ribosomal peptide synthetase, NRPS1 (or pes1), had the highest change in expression between wild type and the SrbA null mutant [43],[44].”
From A Sterol-Regulatory Element Binding Protein Is Required for Cell Polarity, Hypoxia Adaptation, Azole Drug Resistance, and Virulence in Aspergillus fumigatus (2008) · cites this paper as [43]
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Cob-Calan, N. N., Cua-Basulto, M. E., Hernández-Montiel, W., Us-Camas, R. Y., Reyes-Ramírez, A., Dzib-Cauich, D. A., Cristóbal‐Alejo, J., Ruíz-Sánchez, E., & Hernández‐Núñez, E. (2024) · Preprints.org · doi:10.20944/preprints202408.1830.v1 · Cited by 1 · see citing works
Evolution Of Nonribosomal Peptide Synthetase Proteins Involved In Secondary Metabolism In Fungi
Bushley, K. E. (2009) · eCommons (Cornell University) · Cited by 1 · see citing works
Ashraf, S., Dhusia, K., & Verma, S. (2021) · Fungal biology · doi:10.1007/978-3-030-53077-8_4
Revealing Diversity in NRPS Gene Clusters Across Six Pathogenic Colletotrichum Species
Sayari, M., Sharifi-Tehrani, M., Shabani, L., Dolatabadian, A., & Daayf, F. (2025) · Current Microbiology · doi:10.1007/s00284-025-04440-6
- Authors
- Cramer, R. A., Stajich, J. E., Yamanaka, Y., Dietrich, F. S., Steinbach, W. J., & Perfect, J. R.
- Affiliations
- Duke Medical Center (US)
- Corresponding author
- Cramer, Robert A.
- Venue
- Gene
- Publisher
- Elsevier BV
- Published
- 2006-11
- Volume
- 383
- Pages
- 24-32
- ISSN
- 0378-1119 (ISSN-L)
- OpenAlex
- W2020535740
- Cited by
- 66
- References
- 37
- Citations by year
- 2025: 1 · 2024: 2 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 3 · 2018: 1 · 2017: 2 · 2015: 2 · 2014: 3 · 2013: 5 · 2012: 6
- FWCI
- 5.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Gene (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- U.S. Public Health Service (1 K08 A1061149-01)
- National Institute of Allergy and Infectious Diseases (K08AI061149, T32AI052080)
- Topics
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Mycotoxins in Agriculture and Food
- Keywords
- nonribosomal peptide synthetase, Aspergillus, secondary metabolites, adenylation domain, ortholog identification, Aspergillus fumigatus, Aspergillus flavus, Aspergillus terreus, Aspergillus nidulans, Aspergillus oryzae, gene expression, fungal pathogenicity, hidden Markov models
- MeSH terms
- Amino Acid Sequence, Aspergillus, Genes, Fungal, Humans, Molecular Sequence Data, Peptide Synthases, Phylogeny, RNA, Fungal, RNA, Messenger, Sequence Homology, Amino Acid, Protein Structure, Tertiary
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