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Molecular cloning and expression profile analysis of a novel β‐D‐ N ‐acetylhexosaminidase of domestic silkworm ( Bombyx mori )
Author(s) -
Kokuho Takehiro,
Yasukochi Yuji,
Watanabe Satoko,
Inumaru Shigeki
Publication year - 2010
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2010.01401.x
Subject(s) - bombyx mori , biology , bombyx , bombycidae , lepidoptera genitalia , biochemistry , glycan , mannose , sialic acid , homology (biology) , moulting , molecular cloning , microbiology and biotechnology , gene , peptide sequence , glycoprotein , larva , botany
Lepidoptera such as the domestic silkworm ( Bombyx mori ) produce proteins modified with unsialylated, mannose‐rich moieties known as ‘high mannose‐type’ N ‐glycans. However, we observed that, under intrinsic acetylglucosaminidase (GlcNAcase)‐inhibited conditions, moth cells tend to synthesize different types of glycoform with sialic acid modification. To identify molecules essential to assemble Lepidoptera ‐specific N ‐glycans, we performed BLAST analysis on the silkworm genetic database and isolated the entire coding sequence of novel Bombyx GlcNAcase, BmGlcNAcase 2. This enzyme showed weak homology to currently known, lysosome‐associated eukaryotic hexosaminidases, but it revealed remarkable similarity with recently reported glycosyl hydrolases of Spodoptera and Bombyx . Interestingly, BmGlcNAcase 2 was found to be expressed in embryos and in certain tissues of molting larvae (i.e. ovary, fat bodies, mid‐intestine, skin), but not in pupae, suggesting its unique function in the carbohydrate metabolism of juvenile silkworm.