Source:International Journal of Biological Macromolecules, Volume 103
Author(s): Leydianne Leite de Siqueira Patriota, Thamara Figueiredo Procópio, Jéssica de Santana Brito, Virginie Sebag, Ana Patrícia Silva de Oliveira, Ana Karine de Araújo Soares, Leyllane Rafael Moreira, Thâmarah de Albuquerque Lima, Tatiana Soares, Túlio Diego da Silva, Patrícia Maria Guedes Paiva, Virgínia Maria Barros de Lorena, Cristiane Moutinho Lagos de Melo, Lidiane Pereira de Albuquerque, Thiago Henrique Napoleão
In this study, we report the purification and characterization of a multifunctional lectin (MvFL) from Microgramma vacciniifolia fronds as well as its immunomodulatory properties on human peripheral blood mononuclear cells (PBMCs). MvFL (pI 4.51; 54kDa) is a glycoprotein able to inhibit trypsin activity and that has sequence similarities (32% coverage) with a plant RNA-binding protein. Hemagglutinating activity of MvFL was not altered by heating at 100°C for 30min, but was reduced in alkaline pH (8.0 and 9.0). Fluorimetric analyses showed that this lectin did not undergo marked conformational changes when heated. However, the MvFL conformation changed depending on the pH. MvFL at 6.25–25μg/mL was not cytotoxic to lymphocytes present among PBMCs. The PBMCs incubated for 24h with the lectin (12.5μg/mL) showed increased TNF-α, IFN-γ, IL-6, IL-10, and nitric oxide production. MvFL also stimulated T lymphocytes from PBMCs to differentiate into CD8+ cells. The activation (indicated by CD28 expression) of these cells was also stimulated. In conclusion, MvFL is a heat-stable and multifunctional protein, with both lectin and trypsin inhibitor activities, and capable of inducing predominantly a Th1 response in human PBMCs as well as activation and differentiation of T lymphocytes.
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