Apolipophorin-III in Galleria mellonella potentiates hemolymph lytic activity.
Heat-inactivated serum of non-immune Galleria mellonella larvae enhanced the lytic activity of larval cell-free hemolymph against Micrococcus lysodeikticus. The increase in bacterial lysis was due to a 17.2 kDa protein known previously to bind to bacterial lipopolysaccharides. The protein enhanced the lytic activity of insect cell-free hemolymph and hen lysozyme in vitro and insect hemolymph in vivo. The hydrophobic protein, which adhered to M. lysodeikticus, was identified by its amino acid sequence homology as apolipophorin-III. The titer of apolipophorin-III in 200-250 mg last instar larvae was 8.7 mg/ml of hemolymph. Apolipophorin-III did not bind to lysozyme. A possible mode of action of apolipophorin-III with lysozyme in the insect is proposed.
Halwani
A E
AE
Department of Natural Resource Sciences, McGill University, Macdonald Campus, Ste-Anne-de-Bellevue PQ, Canada.
Dunphy
G B
GB
D000595:Amino Acid Sequence; D000818:Animals; D001053:Apolipoproteins / Q000097:blood / Q000276:immunology*; D006458:Hemolymph / Q000276:immunology / Q000502:physiology; D008969:Molecular Sequence Data; D009036:Moths / Q000276:immunology*
D001053:Apolipoproteins; C042470:apolipophorin III