Avian anti-HBV immunoglobulin: New tool to improve hepatitis B diagnosis methods.

Immunoglobulin Y (IgY) could be used in serological diagnosis focused on several infectious agents. This study aims to produce IgY anti-hepatitis B virus surface antigen (anti-HBs) and to assess its use in enzyme immunoassays. Antibodies were produced by immunizing chickens with Hepatitis B vaccine associated (group A), or not, with adjuvant CpG-ODN (group B).

Exploring the potential usefulness of IgY for antiviral therapy: A current review.

Immunoglobulin yolk (IgY) is therapeutic antibodies presented in yolk eggs of birds, reptiles, and amphibians. These proteins produced by the immune system of the animal, are capable of neutralizing antigenic molecules, including viral antigens, fulfilling a role in the body defense. The specificity of these antibodies and the facility for their production, make these molecules capable of being used as tools for diagnosis and immunotherapy.

Comprehensive review on Caelsalpinioideae lectins: From purification to biological activities.

Lectins are a class of proteins with specific and reversible carbohydrate binding properties. Plant lectins constitute the group of these proteins most studied, placing emphasis on the legume family. The Caesalpinioideae subfamily is part of Leguminosae and second only to Papilionoideae with more published works on lectins.

Antinociceptive effect of Lonchocarpus araripensis lectin: activation of L-arginine/NO/cGMP/KATP signaling pathway.

Objective And Design: The involvement of nitric oxide pathway in the antinociceptive activity of Lonchocarpus araripensis lectin (LAL) was investigated in the model of carragenan-induced hypernociception.

Methods: Swiss mice received LAL (0.01-10 mg/kg; i.

The Lectin Isolated from the Alga Hypnea cervicornis Promotes Antinociception in Rats Subjected to Zymosan-Induced Arthritis: Involvement of cGMP Signalization and Cytokine Expression.

This study investigated the effects of the alga lectin Hypnea cervicornis agglutinin (HCA) on rat zymosan-induced arthritis (ZyA). Zymosan (50-500 μg/25 μL) or sterile saline (Sham) was injected into the tibio-tarsal joint of female Wistar rats (180-200 g). Arthritic animals received morphine (4 mg/kg, intraperitoneal), indomethacin (5 mg/kg, intraperitoneal), or 2% lidocaine (100 μL, subcutaneous).

Reviewing Mimosoideae lectins: A group of under explored legume lectins.

Lectins are proteins capable of specific and reversible binding to mono- and/or oligosaccharides, and within this group, Legume lectins are the most studied. However, most of these studies focus on the Papilionoideae subfamily, with Caesalpinioideae and Mimosoideae lectins being significantly less explored in the literature. The Mimosoideae subfamily consists of at least 79 genera and 3275 species, but, to date, only about 14 lectins have been purified, a fact which shows the lack of studies for this group.

Molecular dynamics and binding energy analysis of Vatairea guianensis lectin: a new tool for cancer studies.

The Tn antigen is an epitope containing N-acetyl-D-galactosamine present in the extracellular matrix of some carcinoma cells in humans, and it is often used as a biomarker. Lectins are proteins capable of binding to carbohydrates and can be used as a molecular tool to recognize antigens and to differentiate cancer cells from normal cells. In this context, the present work aimed to characterize the interaction of Vatairea guianensis seed lectin with N-acetyl-D-galactosamine and the Tn antigen by molecular dynamics and molecular mechanics/Poisson-Boltzmann solvent-accessible surface area analysis.

Dalbergieae lectins: A review of lectins from species of a primitive Papilionoideae (leguminous) tribe.

Lectins are (glyco)proteins capable of reversibly binding to specific carbohydrates, thus having various functions and applications. Plant lectins are the best studied, and the Leguminoseae family is highlighted in a number of published works, especially species of the Papilionoideae subfamily. Dalbergieae is one of the tribes in this subfamily comprising 49 genera and over 1300 species.

Purification and partial characterization of a new lectin from Parkia panurensis Benth. ex H.C. Hopkins seeds (Leguminosae family; Mimosoideae subfamily) and evaluation of its biological effects.

Lectins are proteins that have as one of their main characteristics recognizing and reversibly binding to carbohydrates. In this work, it was possible to purify and characterize a lectin from Parkia panurensis (Leguminosae family; Mimosoideae subfamily) seeds by a combination of the techniques: protein precipitation, along with affinity and then ion exchange chromatography using the Sepharose-mannose and diethylaminoethyl matrices, respectively. The pure lectin, called PpaL, has affinity by D-mannose, D-glucose and derivatives.

One century of ConA and 40 years of ConBr research: A structural review.

Lectins are proteins that can bind specifically and reversibly to carbohydrates. This capacity gives lectins multiple biological roles and biotechnological applications. Although lectins can be found in all organisms, plant lectins, especially legume lectins, are undoubtedly the most thoroughly studied.

Lectin purified from Lonchocarpus campestris seeds inhibits inflammatory nociception.

Lonchocarpus campestris (tribe Dalbergieae) possess a mannose biding lectin (LCaL) purified by ion exchange chromatography on DEAE-Sephacel, HiTrap DEAE FF and TSKgel engaged in AKTA-HPLC system. LCaL agglutinates trypsinized rabbit erythrocytes and its activity was maintained after incubation in a wide range of temperature (4-100 °C) and pH (4-9). The lectin had its apparent molecular weight evaluated by size-exclusion chromatography and SDS-PAGE and presented a profile of 10 kDa and 25 kDa in denaturing and native conditions, respectively.

Structural analysis, molecular docking and molecular dynamics of an edematogenic lectin from Centrolobium microchaete seeds.

Lectins represent a class of proteins or glycoproteins capable of reversibly binding to carbohydrates. Seed lectins from the Dalbergieae tribe (Leguminosae) have structural variability, carbohydrate specificity, and biological effects, such as inflammation, vasorelaxation and cancer antigen binding. To comprehensively address these factors, the present work aimed to establish and characterize the three-dimensional structure of Centrolobium microchaete lectin (CML) by homology modeling, investigate protein-carbohydrate interactions and evaluate its inflammatory effect on mice.

Structural analysis of Dioclea lasiocarpa lectin: A C6 cells apoptosis-inducing protein.

Lectins are multidomain proteins that specifically recognize various carbohydrates. The structural characterization of these molecules is crucial in understanding their function and activity in systems and organisms. Most cancer cells exhibit changes in glycosylation patterns, and lectins may be able to recognize these changes.

Canavalia bonariensis lectin: Molecular bases of glycoconjugates interaction and antiglioma potential.

CaBo is a mannose/glucose-specific lectin purified from seeds of Canavalia bonariensis. In the present work, we report the CaBo crystal structure determined to atomic resolution in the presence of X-man, a specific ligand. Similar to the structural characteristics of other legume lectins, CaBo presented the jellyroll motif, a metal binding site occupied by calcium and manganese ions close to the carbohydrate-recognition domain (CRD).

Crystal structure of Pisum arvense seed lectin (PAL) and characterization of its interaction with carbohydrates by molecular docking and dynamics.

The Pisum arvense lectin (PAL), a legume protein belonging to the Vicieae tribe, is capable of specific recognition of mannose, glucose and its derivatives without altering its structure. In this work, the three-dimensional structure of PAL was determined by X-ray crystallography and studied in detail by a combination of molecular docking and molecular dynamics (MD). Crystals belonging to monoclinic space group P2 were grown by the vapor diffusion method at 293 K.

Purification of a thermostable antinociceptive lectin isolated from Andira anthelmia.

Andira anthelmia (tribe Dalbergieae), a plant from Brazilian Amazon, possesses a seed lectin that was purified by affinity chromatography in sepharose-mannose. This novel Dalbergieae lectin, named AAL, agglutinated rabbit erythrocytes treated with trypsin. The hemagglutinating activity of AAL was maintained after incubation at a wide range of temperature (40 to 70 °C) and pH, was shown to be dependent on divalent cations, and was inhibited by d-mannose and d-sucrose.

Effects of Canavalia lectins on acute inflammation in sensitized and non-sensitized rats.

The anti-inflammatory activity of Canavalia seed lectins (Canavalia gladiata [CGL], Canavalia maritima [ConM] and Canavalia brasiliensis [ConBr]) was evaluated by intravenous administration in rats. In non-sensitized rats, cellular edema elicited by carrageenan was reduced (45-51 %) by ConM and (44-59 %) by CGL. Osmotic edema elicited by dextran was reduced by ConM and CGL in 27 % and 29 %.