Abstract
Plants are constantly exposed to a wide range of environmental stresses, but evolved complicated adaptive and defense mechanisms which allow them to survive in unfavorable conditions. These mechanisms protect and defend plants by using different immune receptors located either at the cell surface or in the cytoplasmic compartment. Lectins or carbohydrate-binding proteins are widespread in the plant kingdom and constitute an important part of these immune receptors. In the past years, lectin research has focused on the stress-inducible lectins. The Nicotiana tabacum agglutinin, abbreviated as Nictaba, served as a model for one family of stress-related lectins. Here we focus on three non-chimeric Nictaba homologs from Arabidopsis thaliana, referred to as AN3, AN4, and AN5. Confocal microscopy of ArathNictaba enhanced green fluorescent protein (EGFP) fusion constructs transiently expressed in N. benthamiana or stably expressed in A. thaliana yielded fluorescence for AN4 and AN5 in the nucleus and the cytoplasm of the plant cell, while fluorescence for AN3 was only detected in the cytoplasm. RT-qPCR analysis revealed low expression for all three ArathNictabas in different tissues throughout plant development. Stress application altered the expression levels, but all three ArathNictabas showed a different expression pattern. Pseudomonas syringae infection experiments with AN4 and AN5 overexpression lines demonstrated a significantly higher tolerance of several transgenic lines to P. syringae compared to wild type plants. Finally, AN4 was shown to interact with two enzymes involved in plant defense, namely TGG1 and BGLU23. Taken together, our data suggest that the ArathNictabas represent stress-regulated proteins with a possible role in plant stress responses. On the long term this research can contribute to the development of more stress-resistant plants.
Highlights
Plants are constantly exposed to multiple abiotic and biotic stresses
This study focuses on three Nictaba homologs from Arabidopsis, namely AN3 (AT4G19850.2), AN4 (AT1G31200), and AN5 (AT4G19840)
Alignment of the sequences encoding Nictaba from tobacco and the Nictaba domains from the ArathNictaba sequences showed that the tryptophan residues important for carbohydrate binding activity in Nictaba are conserved in all Nictaba domains
Summary
Plants are constantly exposed to multiple abiotic and biotic stresses. The innate immune system of plants encompasses different immune receptors located either at the cell surface or in the cytoplasmic compartment and allows plants to counteract pathogen attack and survive unfavorable conditions. Evidence has been presented that plant lectins play an important role in the plant innate immune system as immune receptors and/or defense proteins (Peumans and Van Damme, 1995; Lannoo and Van Damme, 2010, 2014). Representative proteins for six out of these lectin families are known as stress-inducible, nucleocytoplasmic lectins. These proteins are low abundant or may even be absent under normal growth conditions, but their expression is elevated when the plant is exposed to stress (Lannoo and Van Damme, 2010)
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