A major endogenous glycosidase mediating quercetin uptake inBombyx mori

Abstract

AbstractQuercetin is a common plant flavonoid that is involved in herbivore–plant interactions. Mulberry silkworms (domestic silkworm,Bombyx mori, and wild silkworm,Bombyx mandarina) uptake quercetin from mulberry leaves and accumulate the metabolites in the cocoon, thereby improving its protective properties. Here we identified and characterized a glycosidase, named LPH-like quercetin glycoside hydrolase 1 (LQGH1), that initiates quercetin metabolism in the domestic silkworm. LQGH1 is expressed in the midgut where it mediates quercetin uptake by deglycosylating the three most common quercetin glycosides present in mulberry leaf: rutin, quercetin-3-O-malonyl-glucoside, quercetin-3-O-glucoside. Despite being located in an unequal crossing-over hotspot,LQGH1is conserved in some species in clade Macroheterocera, including the wild silkworm, indicating the adaptive significance of quercetin uptake.LQGH1is important also in breeding: defective mutations ofLQGH1, which result in discoloration of the cocoon and increased silk yield, are homozygously conserved in 27 of the 32 Japanese white-cocoon domestic silkworm strains and 12 of the 30 Chinese ones we investigated.