Apolipophorin-III and the Interactions of Lipoteichoic Acids with the Immediate Immune Responses of Galleria mellonella

An Insect Multiligand Recognition Protein Functions as an Opsonin for the Phagocytosis of Microorganisms

“…3B). The inhibitory effects of GmCP8 on the binding of DPX to LPS and LTA were similar to or stronger than those of apoLp-III, which was shown previously to bind to LPS and LTA (20,21). It was therefore concluded that GmCP8 could recognize E. coli and M. luteus via specific binding to LPS or LTA.…”

Binding of hemolin to bacterial lipopolysaccharide and lipoteichoic acid. An immunoglobulin superfamily member from insects as a pattern-recognition receptor

“…LPS and LTA are similar in containing both polysaccharide components and lipid components associated with phosphate groups [31], and these may occupy the same binding sites in hemolin. Another insect plasma protein that has been shown to interact with LTA is apolipophorin-III of Galleria mellonella, which presumably binds to the hydrophobic components of LTA [32]. To function as a pattern-recognition receptor, a protein must bind to the surface of invading micro-organisms.…”

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

“…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). Once bound to pathogens or their components, apoLpIII is thought to undergo a conformational change that activates an immune response against the pathogen (Leon et al, 2006;Weers and Ryan, 2006).…”