Manduca sexta lipopolysaccharide-specific immulectin-2 protects larvae from bacterial infection.

Abstract:

:We previously reported the isolation of a lipopolysaccharide (LPS)-specific immulectin-2 from the tobacco hornworm, Manduca sexta [J. Biol. Chem. 275 (2000) 37373]. Immulectin-2 is a C-type lectin that is present at a constitutively low level in hemolymph of naive larvae, and its synthesis is induced after injection of Gram-negative bacteria or LPS. Immulectin-2 contains two carbohydrate recognition domains. It binds to LPS and stimulates prophenoloxidase activation in plasma. In this paper, we focus on properties of carbohydrate recognition domain-2 of immulectin-2 and the biological functions of immulectin-2 in immune responses. The carboxyl-terminal carbohydrate recognition domain (CRD2) of immulectin-2 was able to bind bacterial LPS. Binding of recombinant CRD2 to LPS stimulated activation of prophenoloxidase in plasma. Injection of antiserum against immulectin-2 into M. sexta larvae inhibited clearance of a Gram-negative bacterial pathogen, Serratia marcescens, and decreased survival of infection. These results suggest that immulectin-2 plays an important role in the immune system of M. sexta, and helps to protect the animal from Gram-negative bacterial infections.

journal_name

Dev Comp Immunol

authors

Yu XQ,Kanost MR

doi

10.1016/s0145-305x(02)00099-x

keywords:

subject

Has Abstract

pub_date

2003-03-01 00:00:00

pages

189-96

issue

3

eissn

0145-305X

issn

1879-0089

pii

S0145305X0200099X

journal_volume

27

pub_type

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