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Characterization of a novel Manduca sexta beta-1, 3-glucan recognition protein (?GRP3) with multiple functions.

ABSTRACT: Recognition of pathogens by insect pattern recognition receptors is critical to mount effective immune responses. In this study, we reported a new member (?GRP3) of the ?-1, 3-glucan recognition protein (?GRP) family from the tobacco hornworm Manduca sexta. Unlike other members of the M. sexta ?GRP family proteins, which contain an N-terminal small glucan binding domain and a C-terminal large glucanase-like domain, ?GRP3 is 40-45 residues shorter at the N-terminus and lacks the small glucan binding domain. The glucanase-like domain of ?GRP3 is most similar to that of M. sexta microbe binding protein (MBP) with 78% identity. ?GRP3 transcript was mainly expressed in the fat body, and both its mRNA and protein levels were not induced by microorganisms in larvae. Recombinant ?GRP3 purified from Drosophila S2 cells could bind to several Gram-negative and Gram-positive bacteria and yeast, as well as to laminarin (?-1, 3-glucan), mannan, lipopolysaccharide (LPS), lipoteichoic acid (LTA), and meso-diaminopimelic acid (DAP)-type peptidoglycan (PG), but did not bind to Lysine-type PG. Binding of ?GRP3 to laminarin could be competed well by free laminarin, mannan, LPS and LTA, but almost not competed by free PGs. Recombinant ?GRP3 could agglutinate Bacillus cereus and Escherichia coli in a calcium-dependent manner and showed antibacterial (bacteriostatic) activity against B. cereus, novel functions that have not been reported for the ?GRP family proteins before. M. sexta ?GRP3 may serve as an immune surveillance receptor with multiple functions.


PROVIDER: S-EPMC4143429 | BioStudies | 2014-01-01

REPOSITORIES: biostudies

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