Flexibility of NLPs facilitates attack on plants
Plants are constantly exposed to attacks by various microbes attempting to penetrate their cells. Many pathogens secrete toxic proteins that help with the invasion. One such group of toxins are NLP proteins, cytolysins that damage cell membranes and cause plant tissue death by forming pores in the plasma membrane. Upon contact with the membrane, these toxins bind to the sugar headgroup of specific lipids, glycosylinositol phosphorylceramides (GIPCs), which are embedded in the plasma membrane and act as their targets. Researchers from the Department of Molecular Biology and Nanobiotechnology and the Laboratory for Food Chemistry at the National Institute of Chemistry, together with collaborators, have determined the structure of the sugar headgroup of these lipid targets and explained how NLP toxins recognize them in plant plasma membranes. Using analytical chemistry methods, they isolated different GIPC lipid species with distinct sugar headgroups. Through biophysical methods and molecular simulations, they demonstrated that NLP proteins are remarkably flexible and can adapt their structure to effectively bind various types of lipid receptor sugar headgroups. This structural plasticity enables the toxins to form pores in the membranes of both monocot and dicot plants, which differ in lipid composition. Understanding the mechanisms of membrane binding and pore formation by NLP proteins opens new avenues for developing disease-resistant crops and effective strategies to protect agricultural production from devastating plant pathogens. The study also provides an important piece of the puzzle in explaining why NLP proteins are so widespread in nature and capable of harming many plant species. The authors of the study, published in Science Advances, are: Nika Žibrat Kalanj, Andreja Prešern, Katerina Naumoska, Tina Snoj, Jana Aupič, Vesna Glavnik, Alen Albreht, Mojca Mally, Jure Derganc, Peter Greimel, Alessandra Magistrato, and Gregor Anderluh.
ONLINE LINK: https://www.science.org/doi/10.1126/sciadv.adw6401
CONTACT PERSON: gregor.anderluh@ki.si