Manduca sexta gloverin binds microbial components and is active against bacteria and fungi

Hyalophora gloveri gloverin is a glycine-rich and heat stable antimicrobial protein with activity mainly against Escherichia coli. However, Spodoptera exigua gloverin is active against a Gram-positive bacterium but inactive against E. coli. In this study, we investigated expression profile, binding ability and antimicrobial activity of Manduca sexta gloverin (MsGlv). Msglv transcript was detected in several tissues of naïve larvae with higher levels in the midgut and testis. Expression of Msglv mRNA in larvae was up-regulated by active Spätzle-C108 and peptidoglycans (PGs) of E. coli and Staphylococcus aureus, and the activation was blocked by pre-injection of antibody to M. sexta Toll, suggesting that Msglv expression is regulated by the Toll–Spätzle pathway. Recombinant MsGlv bound to the O-specific antigen and outer core carbohydrate of lipopolysaccharide (LPS), Gram-positive lipoteichoic acid (LTA) and PG, and laminarin, but not to E. coli PG or mannan. MsGlv was active against Bacillus cereus, Saccharomyces cerevisiae and Cryptococcus neoformans, but was almost inactive against E. coli and S. aureus. Our results suggest that gloverins are active against some bacteria and fungi.

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► Msglv expression is up-regulated by Spätzle, Lys-type and DAP-type peptidoglycans.
► Msglv activation by Spätzle and peptidoglycans (PGs) is regulated by the Toll pathway.
► M. sexta gloverin (MsGlv) binds to LPS, Gram-positive LTA and PG, but not to E. coli PG.
► MsGlv binds to the O-specific antigen and outer core carbohydrate moieties of LPS.
► MsGlv is active against some Gram-positive and Gram-negative bacteria, as well as fungi.