Gloverins of the silkworm Bombyx mori: structural and binding properties and activities.

ABSTRACT: Gloverins are basic, glycine-rich and heat-stable antibacterial proteins (∼14- kDa) in lepidopteran insects with activity against Escherichia coli, Gram-positive bacteria, fungi and a virus. Hyalophora gloveri gloverin adopts a random coil structure in aqueous solution but has α-helical structure in membrane-like environment, and it may interact with the lipid A moiety of lipopolysaccharide (LPS). Manduca sexta gloverin binds to the O-specific antigen and outer core carbohydrate of LPS. In the silkworm Bombyx mori, there are four gloverins with slightly acidic to neutral isoelectric points. In this study, we investigate structural and binding properties and activities of B. mori gloverins (BmGlvs), as well as correlations between structure, binding property and activity. Recombinant BmGlv1

SUBMITTER: Yi HY 

PROVIDER: S-EPMC3760519 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature