OsAPSE modulates non-covalent interactions between arabinogalactan protein -glycans and pectin in rice cell walls.

Flexibility of cell walls is crucial to accommodate cell elongation and growth, typically associated with the reorganization of cell wall polysaccharides. Seed germination is a fast-paced developmental process in which cell wall adaptability is highly required. The plant cell utilizes multiple strategies to obtain a flexible cell wall and in part relies on cell wall-active enzymes to loosen both covalent and non-covalent interactions between cell wall polysaccharides.

Novel Lectins from with Differential Glycan Binding Profiles.

The specific interaction of lectins with carbohydrates and glycoconjugates grants these proteins a distinct ability to decode the glycocode. Essential for various biological processes in all organisms, this carbohydrate-binding activity also establishes lectins as valuable tools in fields such as glycomics, medicine, and biotechnology. Considering that the discovery of novel lectins with unique binding profiles is particularly relevant, this study investigated the binding specificity of two lectins extracted from seeds toward simple sugars, -glycans and -glycans.

Novel LacdiNAc-specific lectin from Dioclea reflexa seeds exhibits inflammatory and hypernociceptive properties.

Diocleinae lectins are well known for their prevalent affinity for glycomannosides. However, a rare subset displays specificity towards galactosides. This study describes the characterization of DrfL II, a novel lectin from Dioclea relexa seeds with specificity for N,N'-diacetyl-lactosamine (LacdiNAc).

The future of plant lectinology: Advanced technologies and computational tools.

Lectins play crucial roles in many biological processes and serve as tools in fields ranging from agriculture to biomedicine. While classical methods for lectin discovery and characterization were foundational for the field, they often lack sensitivity and throughput, limiting the detection of less abundant or weakly binding lectins, such as the stress-inducible or monovalent lectins. This review focuses on recent advancements in plant lectin research, particularly novel technologies that complement traditional approaches.

Lectin-carbohydrate analysis by molecular dynamics: Parkia lectins case study.

Understanding lectin-carbohydrate interactions at the structural and molecular levels is crucial to the field of lectins, as the diverse roles and biological activities exhibited by these proteins are fundamentally linked to their specific binding to target glycoconjugates. This study aimed to apply molecular dynamics to analyze the structure and binding properties of Parkia lectins. 3D structures of Parkia platycephala and P.

The crystal structure of Nictaba reveals its carbohydrate-binding properties and a new lectin dimerization mode.

Nictaba is a (GlcNAc)n-binding, stress-inducible lectin from Nicotiana tabacum that serves as a representative for the Nictaba-related lectins, a group of proteins that play pivotal roles in plant defense mechanisms and stress response pathways. Despite extensive research into biological activities and physiological role(s) of the lectin, the three-dimensional structure of Nictaba remained largely unknown. Here, we report crystal structures for Nictaba in the apo form and bound to chitotriose.

Overexpression of the ribosome-inactivating protein modulates the jasmonate signaling pathway in rice.

Ribosome-inactivating proteins (RIPs) are plant enzymes that target the rRNA. The cytoplasmic RIP, called OsRIP1, plays a crucial role in regulating jasmonate, a key plant hormone. Understanding the role of OsRIP1 can provide insights into enhancing stress tolerance and optimizing growth of rice.

Carbohydrate-active enzymes involved in rice cell wall metabolism.

Plant cell walls are complex, multifunctional structures, built up of polysaccharides and proteins. The configuration and abundance of cell wall constituents determine cellular elongation and plant growth. The emphasis of this review is on rice, a staple crop with economic importance, serving as model for grasses/cereals.

Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks.

Background: The CBM13 family comprises carbohydrate-binding modules that occur mainly in enzymes and in several ricin-B lectins. The ricin-B lectin domain resembles the CBM13 module to a large extent. Historically, ricin-B lectins and CBM13 proteins were considered completely distinct, despite their structural and functional similarities.

Computational insights into the circular permutation roles on ConA binding and structural stability.

The mechanisms behind Concanavalin A (ConA) circular permutation have been under investigation since 1985. Although a vast amount of information is available about this lectin and its applications, the exact purpose of its processing remains unclear. To shed light on this, this study employed computer simulations to compare the unprocessed ProConA with the mature ConA.

Jacalin-Curcumin Complex Sensitizes the Breast Cancer MDA-MB-231 Cell Line.

Protein-drug interactions are crucial for understanding drug delivery and cell functions. Jacalin is a suitable molecule for such targeting, as it specifically recognizes the tumor-associated Thomsen-Friedenreich (TF) antigen that is expressed on the glycosylated proteins in cancer cells. The present paper describes the interaction of curcumin and jacalin, a possible carrier molecule for the delivery of antitumor drugs due to its ability to recognize tumor cells.

Structural Analysis and Characterization of an Antiproliferative Lectin from Seeds.

Cells use glycans to encode information that modulates processes ranging from cell-cell recognition to programmed cell death. This information is encoded within a glycocode, and its decoding is performed by carbohydrate-binding proteins. Among these, lectins stand out due to their specific and reversible interaction with carbohydrates.

Agglutinin Prevents Rabies Virus Infection in a Muscle Explant Model.

Infection with the rabies virus (RABV) results in a 100% lethal neurological disease once symptoms develop. Post-exposure prophylaxis (PEP) consists of a combination of vaccination and anti-rabies immunoglobulins (RIGs); it is 100% effective if administered early after exposure. Because of its limited availability, alternatives for RIGs are needed.

Protein interactions during dry and wet heat pre-treatment of skim milk powder (dispersions) and their effect on the heat stability of recombined filled evaporated milk.

Skim milk powder (SMP) as well as aqueous dispersions were subjected to dry and wet heat pre-treatment, respectively, to improve the heat stability of recombined filled evaporated milk (RFEM) derived therefrom. However, microrheological analysis revealed that prolonged incubation caused detrimental effects on the heat stability of RFEM, which were thought to be due to protein interactions. SDS-PAGE results indicated that protein aggregation via non-disulfide covalent bonds occurred upon long-time dry or wet heat incubation.

Plant lectins: Handymen at the cell surface.

Lectins are carbohydrate-binding proteins and are involved in a multitude of biological functions. Lectins at the surface of plant cells often occur as lectin receptor-like kinases (LecRLK) anchored to the plasma membrane. These LecRLKs are part of the plant's pattern-recognition receptor (PRR) system enabling the plant to perceive threats and respond adequately.

Plant lectins as versatile tools to fight coronavirus outbreaks.

The S protein forming the homotrimeric spikes of pathogenic beta-coronaviruses, such as MERS-CoV, SARS-CoV and SARS-CoV-2, is a highly glycosylated protein containing mainly N-glycans of the complex and high-mannose type, as well as O-glycans. Similarly, the host cell receptors DPP4 for MERS-CoV and ACE2 for SARS-CoV and SARS-CoV-2, also represent N- and O-glycosylated proteins. All these glycoproteins share common glycosylation patterns, suggesting that plant lectins with different carbohydrate-binding specificities could be used as carbohydrate-binding agents for the spikes and their receptors, to combat COVID19 pandemics.

A galactoside-specific Dalbergieae legume lectin from seeds of Vataireopsis araroba (Aguiar) Ducke.

The Dalbergieae lectin group encompasses several lectins with significant differences in their carbohydrate specificities and biological properties. The current work reports on the purification and characterization of a GalNAc/Gal-specific lectin from Vataireopsis araroba (Aguiar) Ducke, designated as VaL. The lectin was purified from the seeds in a single step using guar gum affinity chromatography.

Pseudomonas syringae DC3000 infection increases glucosylated N-glycans in Arabidopsis thaliana.

Studying the interaction between the hemibiotrophic bacterium Pseudomonas syringae pv. tomato DC3000 and Arabidopsis thaliana has shed light onto the various forms of mechanisms plants use to defend themselves against pathogen attack. While a lot of emphasis has been put on investigating changes in protein expression in infected plants, only little information is available on the effect infection plays on the plants N-glycan composition.

Differential effects of the recombinant type 1 ribosome-inactivating protein, OsRIP1, on growth of PSB-D and BY-2 cells.

Plant suspension cells were treated with recombinant OsRIP1, a type 1 ribosome-inactivating protein (RIP) from rice ( L.). OsRIP1 triggered cell death in tobacco BY-2 cells but not in PSB-D cells.

Glycosylation-The Most Diverse Post-Translational Modification.

This article is part of the Special Issue Glycosylation-The Most Diverse Post-Translational Modification [...

Carbohydrate-binding protein from stinging nettle as fusion inhibitor for SARS-CoV-2 variants of concern.

agglutinin (UDA) is a carbohydrate-binding small monomeric protein isolated from stinging nettle rhizomes. It inhibits replication of a broad range of viruses, including coronaviruses, in multiple cell types, with appealing selectivity. In this work, we investigated the potential of UDA as a broad-spectrum antiviral agent against SARS-CoV-2.

Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses.

Pathogenic enveloped viruses are covered with a glycan shield that provides a dual function: the glycan structures contribute to virus protection as well as host cell recognition. The three classical types of -glycans, in particular complex glycans, high-mannose glycans, and hybrid glycans, together with some -glycans, participate in the glycan shield of the Ebola virus, influenza virus, human cytomegalovirus, herpes virus, human immunodeficiency virus, Lassa virus, and MERS-CoV, SARS-CoV, and SARS-CoV-2, which are responsible for respiratory syndromes. The glycans are linked to glycoproteins that occur as metastable prefusion glycoproteins on the surface of infectious virions such as gp120 of HIV, hemagglutinin of influenza, or spike proteins of beta-coronaviruses.