Haemolymph proteins of larvae of Galleria mellonella detoxify endotoxins of the insect pathogenic bacteria Xenorhabdus nematophilus (Enterobacteriaceae)

Dunphy, Gary B.; Halwani, Adla E.

doi:10.1016/s0022-1910(97)00072-3

Cited by 71 publications

(47 citation statements)

References 22 publications

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“…In Galleria, two LPS-binding proteins have been identified, and are thought to modulate the LPS-induced inhibition of phenoloxidase in this insect (Dunphy and Halwani, 1997). Binding of LPS to LDL or other haemolymph proteins does not appear to have been investigated in locusts, but it may be that it is its effect on lipid metabolism that is important in the enabling action of AKH on phenoloxidase activation by LPS, but the precise mechanism requires further elucidation.…”

Section: Discussionmentioning

confidence: 99%

Adipokinetic hormone enhances laminarin and bacterial lipopolysaccharide-induced activation of the prophenoloxidase cascade in the African migratory locust, Locusta migratoria

Goldsworthy

Opoku-Ware

Mullen

2002

Journal of Insect Physiology

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Section: Discussionmentioning

confidence: 99%

Adipokinetic hormone enhances laminarin and bacterial lipopolysaccharide-induced activation of the prophenoloxidase cascade in the African migratory locust, Locusta migratoria

Goldsworthy

Opoku-Ware

Mullen

2002

Journal of Insect Physiology

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“…It is thought to act as a pattern recognition molecule (Weers and Ryan, 2006). Apolipophorin III, like lipophorins in mammals (Wendel et al, 2007), can bind and detoxify lipopolysaccharides (LPS) (Dunphy and Halwani, 1997). It also binds to lipoteichoic acid and bacterial surfaces (Halwani et al, 2000), as well as to ␤-1,3-glucans and fungal conidia (Whitten et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Competition between immune function and lipid transport for the protein apolipophorin III leads to stress-induced immunosuppression in crickets

Adamo

Roberts

Easy

et al. 2008

Journal of Experimental Biology

136

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“…ApoLp-III binds to Gram-positive bacteria and to lipoteichoic acid (LTA) (16,17), and as in mammals, apoLp-III can also bind and detoxify LPS (18,19) and promote phagocytosis (20). Furthermore, apoLp-III stimulates increases in hemolymph antibacterial activity (3) and superoxide production by blood cells (hemocytes) (15).…”

mentioning

confidence: 99%

A Novel Role for an Insect Apolipoprotein (Apolipophorin III) in β-1,3-Glucan Pattern Recognition and Cellular Encapsulation Reactions

Whitten

Tew

Lee

et al. 2004

The Journal of Immunology

203

163

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Lipoproteins and molecules for pattern recognition are centrally important in the innate immune response of both vertebrates and invertebrates. Mammalian apolipoproteins such as apolipoprotein E (apoE) are involved in LPS detoxification, phagocytosis, and possibly pattern recognition. The multifunctional insect protein, apolipophorin III (apoLp-III), is homologous to apoE. In this study we describe novel roles for apoLp-III in pattern recognition and multicellular encapsulation reactions in the innate immune response, which may be of direct relevance to mammalian systems. It is known that apoLp-III stimulates antimicrobial peptide production in insect blood, enhances phagocytosis by insect blood cells (hemocytes), and binds and detoxifies LPS and lipoteichoic acid. In the present study we show that apoLp-III from the greater wax moth, Galleria mellonella, also binds to fungal conidia and β-1,3-glucan and therefore may act as a pattern recognition molecule for multiple microbial and parasitic invaders. This protein also stimulates increases in cellular encapsulation of nonself particles by the blood cells and exerts shorter term, time-dependent, modulatory effects on cell attachment and spreading. All these responses are dose dependent, occur within physiological levels, and, with the notable exception of β-glucan binding, are only observed with the lipid-associated form of apoLp-III. Preliminary studies also established a beneficial role for apoLp-III in the in vivo response to an entomopathogenic fungus. These data suggest a wide range of immune functions for a multiple specificity pattern recognition molecule and may provide a useful model for identifying further potential roles for homologous proteins in mammalian immunology, particularly in terms of fungal infections, pneumoconiosis, and granulomatous reactions.

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Haemolymph proteins of larvae of Galleria mellonella detoxify endotoxins of the insect pathogenic bacteria Xenorhabdus nematophilus (Enterobacteriaceae)

Cited by 71 publications

References 22 publications

Adipokinetic hormone enhances laminarin and bacterial lipopolysaccharide-induced activation of the prophenoloxidase cascade in the African migratory locust, Locusta migratoria

Adipokinetic hormone enhances laminarin and bacterial lipopolysaccharide-induced activation of the prophenoloxidase cascade in the African migratory locust, Locusta migratoria

Competition between immune function and lipid transport for the protein apolipophorin III leads to stress-induced immunosuppression in crickets

A Novel Role for an Insect Apolipoprotein (Apolipophorin III) in β-1,3-Glucan Pattern Recognition and Cellular Encapsulation Reactions

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