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Screening of Bombyx mori brain proteins interacting with protein tyrosine phosphatase of BmNPV
Author(s) -
Wang Guobao,
Na Shuang,
Qin Li
Publication year - 2020
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21732
Subject(s) - bombyx mori , biology , protein tyrosine phosphatase , cyclophilin , phosphatase , biochemistry , protein subunit , microbiology and biotechnology , tyrosine , enzyme , gene
In this study, glutathione‐S‐transferase pull‐down combined with mass spectrometry techniques were used to identify the candidate proteins interacting with protein tyrosine phosphatase of the Bombyx Mori nucleopolyhedrovirus in the B. mori (BmNPV‐PTP) brain. A total of 36 proteins were identified from BmNPV‐PTP coprecipitate samples by searching the NCBI_ Bombyx Mori database with the original mass spectrum data. Among those proteins, the interaction between BmNPV‐PTP and B. mori cyclophilin A may accelerate the apoptosis of certain nerve cells involved in regulating behavior, and thus may be an inducer of enhanced locomotor activity (ELA). After the BmNPV invasion, BmNPV‐PTP binding to peripheral‐type benzodiazepine receptors may initiate a series of abnormal cascades of the nervous system, which results in abnormal hyperactive behavior in B. mori . Besides this, vacuolar ATP synthase catalytic subunit A, annexin, and several enzymes for energy conversion were identified, which may play a role in enhancing viral entry and infectivity and provide energy for enhancing the locomotor activity of B. mori . In general, the results of this study will facilitate the understanding of the molecular mechanisms underlying the ELA of B. mori larva induced by BmNPV.