Evidence for a LPS‐binding protein in medfly hemocyte surface: Mediation in LPS internalization but not in LPS signaling

Metheniti, Aristea; Giannakas, Nikos; Katsoulas, Haralabos L.; Soldatos, Anastasios N.; Tsakas, Sotiris; Lambropoulou, María

doi:10.1002/arch.10096

Cited by 3 publications

(3 citation statements)

References 34 publications

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“…The hydrophobic tail of tGNBP-2 is highly homologous to the tail of Drosophila GNBP (20) and therefore likely serves as a GPI anchor. Existence in both soluble and membrane-associated forms is common among pattern receptors including mammalian CD14 (21) and various insect proteins (22).…”

Section: Resultsmentioning

confidence: 99%

Targeting an antimicrobial effector function in insect immunity as a pest control strategy

Bulmer

Bachelet

Raman

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

142

124

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Insect pests such as termites cause damages to crops and manmade structures estimated at over $30 billion per year, imposing a global challenge for the human economy. Here, we report a strategy for compromising insect immunity that might lead to the development of nontoxic, sustainable pest control methods. Gramnegative bacteria binding proteins (GNBPs) are critical for sensing pathogenic infection and triggering effector responses. We report that termite GNBP-2 (tGNBP-2) shows ␤(1,3)-glucanase effector activity previously unknown in animal immunity and is a pleiotropic pattern recognition receptor and an antimicrobial effector protein. Termites incorporate this protein into the nest building material, where it functions as a nest-embedded sensor that cleaves and releases pathogenic components, priming termites for improved antimicrobial defense. By means of rational design, we present an inexpensive, nontoxic small molecule glycomimetic that blocks tGNBP-2, thus exposing termites in vivo to accelerated infection and death from specific and opportunistic pathogens. Such a molecule, introduced into building materials and agricultural methods, could protect valuable assets from insect pests.␤(1,3)-glucanase ͉ Gram-negative bacteria binding proteins ͉ pattern recognition receptor ͉ termites ͉ social insect immunity

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Section: Resultsmentioning

confidence: 99%

Targeting an antimicrobial effector function in insect immunity as a pest control strategy

Bulmer

Bachelet

Raman

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

142

124

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“…In the absence of plasma factors/proteins in the in vitro cell culture, very little bacterial components bound to hemocytes and fat body, resulting in low activation level of AMPs. Plasma proteins with such functions may include C-type lectins, PGRPs and beta-glucan recognition/Gram negative bacteria binding proteins, which have the ability to bind LPS, LTA and PG (Ao et al, 2008a; Jomori and Natori, 1991; Lee et al, 2000; Metheniti et al, 2003; Xu et al, 1995; Yu and Kanost, 2002; Yu et al, 2006). …”

Section: Discussionmentioning

confidence: 99%

Lipoteichoic acid and lipopolysaccharide can activate antimicrobial peptide expression in the tobacco hornworm Manduca sexta

Rao

2010

Developmental & Comparative Immunology

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Activation of prophenoloxidase and synthesis of antimicrobial peptides (AMPs) are two important innate immune mechanisms in insects. In the current study, we investigated immune responses activated by three major bacterial components, lipopolysaccharide (LPS) (including rough mutants of LPS), lipoteichoic acid (LTA), and peptidoglycan (PG), in the larvae of a lepidopteran insect, Manduca sexta. We found that two DAP (Diaminopimelic acid)-type PGs from Escherichia coli and Bacillus subtilis were much more potent than LPS and LTA from the respective bacteria as well as a Lysine-type PG in activation of prophenoloxidase in M. sexta larval plasma in vitro. Transcription levels of AMP genes, such as Attacin, Lebocin and Moricin genes, in the hemocytes and fat body of larvae were significantly induced by smooth LPS (TLR4grade) and rough mutants of LPS (TLRgrade ™ ), synthetic lipid A, LTA, and PG. LPS from E. coli and LTA from B. subtilis activated AMP expression to significantly higher levels than PGs from the respective bacterial strains, and smooth LPS were more potent than lipid A and rough mutants of LPS in activation of AMP expression. Our results demonstrated for the first time that LTA can activate AMP expression, and different moieties of LPS may synergistically activate AMP expression in M. sexta.

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“…Lipid A, a stimulatory center for mammalian immune systems, binds to the Toll-like receptor 4-MD2 complex, leading to the production of proinflammatory cytokines (Miyake, 2004). The active center of LPS in insects has not been determined, even though LPS stimulates various immune responses, activates the pro-phenoloxidase (PPO) cascade (Yu and Kanost, 2003), enhances cellular immune reactions (Koizumi et al, 1997;Metheniti et al, 2003;Soldatos et al, 2003), and causes the production of nitric oxide (Imamura et al, 2002;Krishnan et al, 2005) and the transcriptional activation of antimicrobial peptide genes (Furukawa et al, 1999;Seitz et al, 2003). In the silkworm Bombyx mori, LPS is a strong elicitor of several antibacterial peptide genes.…”

Section: Introductionmentioning

confidence: 99%

Verification of elicitor efficacy of lipopolysaccharides and peptidoglycans on antibacterial peptide gene expression in Bombyx mori

Lee

Noda

et al. 2007

Insect Biochemistry and Molecular Biology

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Evidence for a LPS‐binding protein in medfly hemocyte surface: Mediation in LPS internalization but not in LPS signaling

Cited by 3 publications

References 34 publications

Targeting an antimicrobial effector function in insect immunity as a pest control strategy

Targeting an antimicrobial effector function in insect immunity as a pest control strategy

Lipoteichoic acid and lipopolysaccharide can activate antimicrobial peptide expression in the tobacco hornworm Manduca sexta

Verification of elicitor efficacy of lipopolysaccharides and peptidoglycans on antibacterial peptide gene expression in Bombyx mori

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