4.6 Article

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

Journal

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume 40, Issue 10, Pages 713-722

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.ibmb.2010.07.002

Keywords

Leucine-rich repeat; Lipopolysaccharide; Hemolymph; Hemocyte; Innate immunity; Insect; Manduca sexta

Funding

  1. NIGMS NIH HHS [R37 GM041247, R01 GM041247] Funding Source: Medline

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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. (C) 2010 Elsevier Ltd. All rights reserved.

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