ArticleThe Plant cell2009
The O-mannosyltransferase PMT4 is essential for normal appressorium formation and penetration in Ustilago maydis.
Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed, 73 citations in OpenAlex.
- Protein Extraction Methods for Ustilago maydis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Integrative perspectives on glycosylation networks in fungi and oomycetes.Journal of microbiology (Seoul, Korea) · 2025Review
- Pmt4 recognizes two separate acceptor sites to O-mannosylate in the S/T-rich regions of substrate proteins.Nature communications · 2025Article
- Integrative glycomic analysis reveals the crucial role of protein glycosylation in fungal pathogenesis.PLoS pathogens · 2025Article
- Article
- N-glycosylation of the envelope glycoprotein I is essential for the proliferation and virulence of the duck plague virus.Veterinary research · 2024Article
- Article
- Progress in pathogenesis research of Ustilago maydis, and the metabolites involved along with their biosynthesis.Molecular plant pathology · 2023Review
- Article
- Transcriptome Comparison between Two Strains ofJournal of fungi (Basel, Switzerland) · 2022Article
- Biotoxicity assessment of cloned cry 11 protein gene fromSaudi journal of biological sciences · 2022Article
- Secreted Glycosyltransferase RsIA_GT ofPathogens (Basel, Switzerland) · 2022Article
- Comparative Secretome Analysis of Magnaporthe oryzae Identified Proteins Involved in Virulence and Cell Wall Integrity.Genomics, proteomics & bioinformatics · 2022Article
- Article
- Article
- Structural, Evolutionary, and Functional Analysis of the Protein O-Mannosyltransferase Family in Pathogenic Fungi.Journal of fungi (Basel, Switzerland) · 2021Review
- N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence.PLoS pathogens · 2019Article
- MaPmt4, a protein O-mannosyltransferase, contributes to cell wall integrity, stress tolerance and virulence in Metarhizium acridum.Current genetics · 2019Article
- Signal peptide peptidase activity connects the unfolded protein response to plant defense suppression by Ustilago maydis.PLoS pathogens · 2019Article
- Pleiotropic roles of O-mannosyltransferase MoPmt4 in development and pathogenicity of Magnaporthe oryzae.Current genetics · 2019Article
Corrections and comments
- Commented on by
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Saccharomyces cerevisiae, the PMT, KRE2/MNT1, and MNN1 mannosyltransferase protein families catalyze the steps of the O-mannosylation pathway, sequentially adding mannoses to target proteins. We have identified members of all three families and analyzed their roles in pathogenesis of the maize smut fungus Ustilago maydis. Furthermore, we have shown that PMT4, one of the three PMT family members in U. maydis, is essential for tumor formation in Zea mays. Significantly, PMT4 seems to be required only for pathogenesis and is dispensable for other aspects of the U. maydis life cycle. We subsequently show that the deletion of pmt4 results in a strong reduction in the frequency of appressorium formation, with the few appressoria that do form lacking the capacity to penetrate the plant cuticle. Our findings suggest that the O-mannosylation pathway plays a key role in the posttranslational modification of proteins involved in the pathogenic development of U. maydis. The fact that PMT homologs are not found in plants may open new avenues for the development of fungal control strategies. Moreover, the discovery of a highly specific requirement for a single O-mannosyltransferase should aid in the identification of the proteins directly involved in fungal plant penetration, thus leading to a better understanding of plant-fungi interactions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.