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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.

With the developing of Distributed Database technology, fuzzy query of Distributed Database has been playing an important role in the information query. Raising query speed and precision ratio is always the main topic of information query. In this paper, a new type of information query system--Distributed Database system is designed with rough set theory and fuzzy set knowledge. A new information query method is advanced and the architecture of the system and its key algorithms are given. Main characteristic of the research achievement is that query algorithm’s time complexity decreases with the increase of amount of information and relates to the only amount of index words. Results show that it is an effective method with which a system for fuzzy query is implemented.

Here, we assessed the effect of a systematic change in reactive center loop (RCL) length, N‐terminal to the reactive center, on the inhibitory activity of the recombinant Apserpin‐6. The domain prediction results indicated that the RCL is located between the amino acid numbered 359–379 at the C‐terminal of Apserpin‐6. The N‐terminal variable region for amino acid positions P7–P1 of the RCL of Apserpin‐6 was truncated or extended by residue deletion or insertion using site‐directed mutagenesis. The recombinant Apserpin‐6 with one or two residues insertion in RCL had no effect on prophenoloxidase (proPO) activity, whereas deletion of one or two residues in RCL lowered the efficiency of inhibition of Apserpin‐6. The results of this study will facilitate the understanding of inhibition mechanism of RCL on proPO activity.