ArticleJournal of experimental botany2018
The major nectar protein of Brassica rapa is a non-specific lipid transfer protein, BrLTP2.1, with strong antifungal activity.
Article in Journal of experimental botany, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 54 citations in OpenAlex.
- Cysteine-Rich Peptides in Food Systems: Structure, Sources, Functional Properties, Potential Applications, and Future Perspectives.Probiotics and antimicrobial proteins · 2026Review
- Localization and Functional Analysis of CtLTP8, an Extracellular Vesicle Protein That Enhances Resistance toPlants (Basel, Switzerland) · 2026Article
- Fine Mapping of thePlants (Basel, Switzerland) · 2026Article
- Nectary starch degradation affects nectar chemical composition, but not nectar sugars, in Arabidopsis thaliana.Plant physiology · 2025Article
- Nectar peroxide: assessing variation among plant species, microbial tolerance, and effects on microbial community assembly.The New phytologist · 2025Article
- Lipid transfer protein VAS inhibits the hypersensitive response via reactive oxygen species signaling in Nicotiana benthamiana.Journal of experimental botany · 2025Article
- Seasonal Assembly of Nectar Microbial Communities Across Angiosperm Plant Species: Assessing Contributions of Climate and Plant Traits.Ecology letters · 2025Article
- Specialized metabolites present inFrontiers in plant science · 2025Article
- Roles of non-specific lipid transfer proteins in plant defense: structural and functional perspectives.Frontiers in fungal biology · 2025Review
- Antimicrobial Plant Peptides: Structure, Classification, Mechanism and Therapeutic Potential.Current topics in medicinal chemistry · 2025Review
- Article
- Lipid transfer protein StLTPa enhances potato disease resistance against different pathogens by binding and disturbing the integrity of pathogens plasma membrane.Plant biotechnology journal · 2024Article
- Link between organic nanovescicles from vegetable kingdom and human cell physiology: intracellular calcium signalling.Journal of nanobiotechnology · 2024Article
- Identification and evolution of nsLTPs in the root nodule nitrogen fixation clade and molecular response of Frankia to AgLTP24.Scientific reports · 2023Article
- Nectar compounds impact bacterial and fungal growth and shift community dynamics in a nectar analog.Environmental microbiology reports · 2023Article
- Lipid transfer proteins involved in plant-pathogen interactions and their molecular mechanisms.Molecular plant pathology · 2022Review
- Lipid Transfer Proteins (LTPs)-Structure, Diversity and Roles beyond Antimicrobial Activity.Antibiotics (Basel, Switzerland) · 2021Review
- Integrative analysis of transcriptome and proteome revealed nectary and nectar traits in the plant-pollinator interaction of Nitraria tangutorum Bobrov.BMC plant biology · 2021Article
- Speaking the language of lipids: the cross-talk between plants and pathogens in defence and disease.Cellular and molecular life sciences : CMLS · 2021Review
- Structural characterization and in vitro lipid binding studies of non-specific lipid transfer protein 1 (nsLTP1) from fennel (Foeniculum vulgare) seeds.Scientific reports · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nectar is one of the key rewards mediating plant-mutualist interactions. In addition to sugars, nectars often contain many other compounds with important biological functions, including proteins. This study was undertaken to assess the proteinaceous content of Brassica rapa nectar. SDS-PAGE analysis of raw B. rapa nectar revealed the presence of ~10 proteins, with a major band at ~10 kDa. This major band was found to contain a non-specific lipid transfer protein encoded by B. rapa locus Bra028980 and subsequently termed BrLTP2.1. Sequence analysis of BrLTP2.1 predicted the presence of a signal peptide required for secretion from the cell, eight cysteines, and a mature molecular mass of 7.3 kDa. Constitutively expressed BrLTP2.1-GFP in Arabidopsis displayed accumulation patterns consistent with secretion from nectary cells. BrLTP2.1 was also found to have relatively high sequence similarity to non-specific lipid-transfer proteins with known functions in plant defense, including Arabidopsis DIR1. Heterologously expressed and purified BrLTP2.1 was extremely heat stable and bound strongly to saturated free fatty acids, but not methyl jasmonate. Recombinant BrLTP2.1 also had direct antimicrobial activity against an extensive range of plant pathogens, being particularly effective against necrotrophic fungi. Taken together, these results suggest that BrLTP2.1 may function to prevent microbial growth in nectars.
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