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5. The Differential Expression of BmGlcNAcase2 in Strains of Bombyx mori (Lepidoptera: Bombycidae) With Different Susceptibility to Bombyx mori (Lepidoptera: Bombycidae) Nucleopolyhedrovirus Infection

Author

Liu XiaoYong, Zhu Hao, and Ma Quanbing

Subjects
β-N-acetylglucosaminidase2, viruses, resistance, Bombycidae, Lepidoptera genitalia, Open Reading Frames, Bombyx mori, Acetylglucosaminidase, Hydrolase, Animals, Missense mutation, RNA, Messenger, Bombyx, biology, Strain (chemistry), Research, fungi, General Medicine, biology.organism_classification, Virology, Molecular biology, Nucleopolyhedroviruses, enzyme activity, Open reading frame, Gene Expression Regulation, Larva, Insect Science, Insect Proteins, nucleopolyhedrovirus
Abstract

GlcNAcase is a glycosyl hydrolase located in the lysosomes of numerous organisms. Levels of the protein, β-N-acetylglucosaminidase 2 (GlcNAcase2), which is a member of the GlcNAcase family, are different in two strains of the silkworm Bombyx mori that have different resistance to Bombyx mori nucleopolyhedroviruses (BmNPVs). We identified six single-nucleotide differences in the GlcNAcase2 coding sequence between the 306 and NB strains. Five are silent changes, but one is a nonsynonymous mutation. Reverse transcription-polymerase chain reaction analysis showed that GlcNAcase2 mRNA levels in the NB strain were nearly 2.57 times higher compared with those in the 306 strain. In addition, GlcNAcase2 enzyme activity was much higher in the NB strain compared with that in the 306 strain. Together, these results indicate that GlcNAcase2 may be involved in variable BmNPV resistance in B. mori.

Published
2015

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