Apolipophorin-III in Galleria mellonella potentiates hemolymph lytic activity

Halwani, Adla E.; Dunphy, Gary B.

doi:10.1016/s0145-305x(99)00037-3

Cited by 76 publications

(42 citation statements)

References 18 publications

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“…Wiesner et al, 1997;Halwani and Dunphy, 1999;Kim et al, 2004). Wiesner et al (Wiesner et al, 1997) found that the greater the amount of apoLpIII injected, the greater the increase in antibacterial activity in the hemolymph.…”

Section: Discussionmentioning

confidence: 99%

“…To determine whether injecting apoLpIII could reverse flightinduced immunosuppression, apoLpIII was isolated from cricket hemolymph using a procedure modified from published methods Halwani and Dunphy, 1999). Hemolymph was collected by making a shallow incision in the pronotal membrane and removing the hemolymph that welled up from the wound (approx.…”

Section: The Effect Of Pre-loading With Apolpiii On Flight-induced Immentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: The Effect Of Pre-loading With Apolpiii On Flight-induced Immentioning

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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“…Finally, the effect of the length of the in vivo incubation time for injected apoLp-III was also tested using 20 l of 1.0 mg/ml apoLp-III, and hemocyte samples were taken at 20, 40, or 60 min postinjection and treated as described above. All incubation times were selected on the basis of results from preliminary optimization experiments, and the apoLp-III concentrations used represent physiological levels (16).…”

Section: Effects On Plasmatocyte Spreading On Glassmentioning

confidence: 99%

“…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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“…A further component of the lipid transport system, the exchangeable apolipophorin III (apoLp-III) has immune-stimulating ability in Galleria (Weisner et al, 1997;Halwani et al, 1999;Dettloff et al, 2001a). Two bacterial lipopolysaccharide (LPS) binding proteins were isolated from Galleria haemolymph, one of which may correspond to apoLp-III, based on its molecular weight (Dunphy & Halwani, 1997).…”

Section: Introductionmentioning

confidence: 99%

Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens

Mullen

Goldsworthy

2003

Insect Biochemistry and Molecular Biology

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Apolipophorin-III in Galleria mellonella potentiates hemolymph lytic activity

Cited by 76 publications

References 18 publications

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

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

Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens

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