Revisiting proteus:: Do minor changes in lectin structure matter in biological activity?: Lessons from and potential biotechnological uses of the diocleinae subtribe lectins

被引:113
作者
Cavada, BS
Barbosa, T
Arruda, S
Grangeiro, TB
Barral-Netto, M
机构
[1] Fiocruz MS, Lab Imunoregulacao & Microbiol, LIMI, BR-40295001 Salvador, BA, Brazil
[2] Univ Fed Ceara, Dept Bioquim & Biol Mol, Biomol Lab, BR-60451970 Fortaleza, Ceara, Brazil
[3] Univ Fed Ceara, Dept Biol, Lab Citogenet & Genet Mol, BR-60451970 Fortaleza, Ceara, Brazil
关键词
D O I
10.2174/1389203013381152
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
Significant differences in function have been observed among lectins structurally similar to concanavalin A, but their high homology with this widely used lectin has kept them in obscurity. The observation of large differences in the potency of many of these Diocleinae lectins as stimulators of Interferon-gamma production by human peripheral blood mononuclear cells has lead to a major effort to unravel their chemical structure and biological activity. Modeling studies of some of these lectins reveal conformational changes in side chains of some residues involved in the carbohydrate-binding site, with possible effects on the ability of these proteins to recognize specific carbohydrate structures. Additionally, all them constitute in fact a mixture of isolectins, which in different proportions could lead to diverse effects. The present review of the biological actions of Diocleinae lectins includes several in vitro and in vivo immunological findings, as well as their effects on insect growth and reproduction. In these systems Diocleinae lectins proved to be quite diverse in their potency, Such diversity in the biological activity of highly related proteins recalls the origin of the name protein: like Proteus, the capability of assuming various forms is the essential feature of this class of molecules.
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页码:123 / 135
页数:13
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