Leureptin: A soluble, extracellular leucine-rich repeat protein from Manduca sexta that binds lipopolysaccharide

Leucine-rich repeat containing proteins are involved in immune response in many capacities. In insects, these include Toll-like receptors and the Anopheles gambiae proteins APL1 and LRIM1. Here we describe the identification and characterization of leureptin, a novel extracellular protein with 13 leucine-rich repeats from hemolymph of the insect Manduca sexta. After injection of bacteria, leureptin mRNA level increased in fat body, but protein levels in plasma decreased, an indication that leureptin is consumed during the immune response. Leureptin bound to bacterial lipopolysaccharide (LPS). Microscopy using leureptin antiserum showed that leureptin associates with hemocytes after injection of bacteria, an indication that leureptin is involved in hemocyte responses to bacterial infection. Sequence database searches suggest similar proteins are present in other Lepidopteran species.

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► Leureptin, a hemolymph plasma protein from Manduca sexta, contains 13 leucine-rich repeats. Leureptin mRNA levels increase in fat body after bacterial injection but protein levels in plasma decrease, suggesting leureptin is consumed during the immune response. Leureptin binds to bacterial lipopolysaccharide and associates with hemocytes after injection of bacteria.