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PeerJ. 2018 Sep 21;6:e5658. doi: 10.7717/peerj.5658. eCollection 2018.

A secretory hexokinase plays an active role in the proliferation of Nosema bombycis.

Huang Y1, Zheng S1, Mei X1, Yu B1, Sun B1, Li B1, Wei J1,2, Chen J1,2, Li T1,2, Pan G1,2, Zhou Z1,2,3, Li C1,2.

Author information

State Key Laboratory Of Silkworm Genome Biology, Southwest University, Chongqing, Chongqing, China.
Southwest University, Key Laboratory for Sericulture Functional Genomics and Biotechnology of Agricultural Ministry, Chongqing, Chongqing, China.
Chongqing Normal University, College of Life Sciences, Chongqing, Chongqing, China.


The microsporidian Nosema bombycis is an obligate intracellular parasite of Bombyx mori, that lost its intact tricarboxylic acid cycle and mitochondria during evolution but retained its intact glycolysis pathway. N. bombycis hexokinase (NbHK) is not only a rate-limiting enzyme of glycolysis but also a secretory protein. Indirect immunofluorescence assays and recombinant HK overexpressed in BmN cells showed that NbHK localized in the nucleus and cytoplasm of host cell during the meront stage. When N. bombycis matured, NbHK tended to concentrate at the nuclei of host cells. Furthermore, the transcriptional profile of NbHK implied it functioned during N. bombycis' proliferation stages. A knock-down of NbHK effectively suppressed the proliferation of N. bombycis indicating that NbHK is an important protein for parasite to control its host.


Hexokinase; Microsporidia; RNAi; Secretory protein

Conflict of interest statement

The authors declare there are no competing interests.

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