No description available.

Apolipophorin-III (apoLp-III) is known to influence the haemocyte-mediated induction of antimicrobial peptides in Galleria mellonella and yeast phagocytosis, bind to Gram-negative and Gram positive bacteria and limit the activation of the haemocytes and the prophenoloxidase system by bacterial surface antigens. The effects of apoLp-III on haemocyte adhesion to glass slides and to bacteria were herein examined. ApoLp-III bound to haemocytes limiting the adhesion of both granular cells and plasmatocytes to glass and the contact of the plasmatocytes with Bacillus subtilis. The percentage of granular cells with bacteria was increased by the protein. However, the total number of bacteria adhering to haemocytes in vitro declined in the presence of apoLp-III. Bacterial removal from the haemolymph in vivo by the haemocytes was slowed by the protein. / The adhesion of both the granular cells and plasmatocytes to slides was decreased by inhibiting protein tyrosine kinase and increased by inhibiting protein kinase A (PKA) and protein kinase C (PKC) activity. The latter was confirmed with haemocytes inhibited by the general PKC inhibitor H-7 using phorbol-3-myfstate (PMA) which, by activating PKC, diminished the adhesion of both haemocyte types. Limiting the formation of PKC activation by diacylglycerides which is produced by phosholipase C (PLC), using PLC inhibitor also increased haemocyte attachment. Although binding of B. subtilis to haemocytes decreased PKC activity, the effect of apoLp-III on PKC was inconclusive.

No description available.

Apolipophorin-III is a hemolymph protein known for its role in lipid transport. Apolipophorin-III isolated from the hemolymph of last instar larvae of Galleria mellonella bound to the surface of the insect pathogenic Gram-negative bacterium Xenorhabdus nematophilus and to the lipid A moiety of its lipopolysaccharide. This binding reduced the toxicity of the lipopolysaccharide to hemocytes and decreased the inhibitory effect of the lipopolysaccharide on phenoloxidase. Apolipophorin-III also bound to the Gram-positive bacterium Micrococcus lysodeikticus; this enhanced the activity of hen egg lysozyme on the organism as well as the lytic activity of G. mellonella cell-free hemolymph. / The involvement of apolipophorin-III in the immune responses of G. mellonella larvae to lipoteichoic acids, surface components of Gram-positive bacteria, was examined. Lipoteichoic acids from Bacillus subtilis, Enterococcus hirae and Streptococcus pyogenes caused a dose- and time-dependent drop in the total counts of circulating hemocytes and a partial or complete depletion of plasmatocytes depending on the species of lipoteichoic acid. All lipoteichoic acids tested activated phenoloxidase in vitro; however, in vivo, only B. subtilis lipoteichoic acid elevated the phenoloxidase activity while the other two suppressed it. Binding of apolipophorin-III to lipoteichoic acids was demonstrated. Apolipophorin-III prevented the complete depletion of plasmatocytes and depressed the activation of phenoloxidase by lipoteichoic acid from B. subtilis. The concentration of apolipophorin-III in hemolymph two hours post injections of lipopolysaccharides or lipoteichoic acids into larvae of G. mellonella did not change with respect to control insects that received phosphate-buffered saline. The concentration of apolipophorin-III in hemolymph at the end of the feeding larval stage was 8--12 mg/mL of hemolymph. Apolipophorin-III was present in significant amounts in the prepupal, pupal and adult stages. The protein was detected immunologically in hemocyte lysates, plasma and fat body. Non-denaturing polyacrylamide gels and immunoblots of fresh hemolymph suggested that apolipophorin-III is associated with a 77 kDa protein.