Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)

Plutella xylostella L. (diamondback moth) is a pest of cruciferous plants. To understand the relationship among protease inhibitors, protease activities and the growth and development of this insect, the activities of midgut proteases of P. xylostella larvae were determined in this study. Protease s...

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Main Authors: Aiping Zhao, Yin Li, Chunmeng Leng, Ping Wang, Yiping Li
Format: Article
Language:English
Published: Frontiers Media S.A. 2019-01-01
Series:Frontiers in Physiology
Subjects:
Online Access:https://www.frontiersin.org/article/10.3389/fphys.2018.01963/full
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spelling doaj-244a4e9a9c094190aaa9fe4cafbda2ee2020-11-25T01:28:58ZengFrontiers Media S.A.Frontiers in Physiology1664-042X2019-01-01910.3389/fphys.2018.01963403843Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)Aiping Zhao0Aiping Zhao1Yin Li2Yin Li3Chunmeng Leng4Chunmeng Leng5Ping Wang6Yiping Li7Yiping Li8Key Laboratory of Plant Protection Resources and Pest Management, Ministry of Education, Northwest A&F University, Yangling, ChinaState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, ChinaKey Laboratory of Plant Protection Resources and Pest Management, Ministry of Education, Northwest A&F University, Yangling, ChinaState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, ChinaKey Laboratory of Plant Protection Resources and Pest Management, Ministry of Education, Northwest A&F University, Yangling, ChinaState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, ChinaDepartment of Entomology, Cornell University, Ithaca, NY, United StatesKey Laboratory of Plant Protection Resources and Pest Management, Ministry of Education, Northwest A&F University, Yangling, ChinaState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, ChinaPlutella xylostella L. (diamondback moth) is a pest of cruciferous plants. To understand the relationship among protease inhibitors, protease activities and the growth and development of this insect, the activities of midgut proteases of P. xylostella larvae were determined in this study. Protease samples were extracted from the midguts of P. xylostella larvae, and the protease activities were determined using enzyme specific substrates. The results showed that CaCl2, EDTA, and EGTA inhibited only the trypsin. Among the common protease inhibitors, phenylmethyl sulfonyl fluorine (PMSF), Nα-p-methyl sulfonyl-L-lysine chloromethylketone (TLCK), Nα-methyl sulfonyl-L- phenylalanine chloromethyl ketone (TPCK), soybean trypsin inhibitor (STI), and PMSF inhibited the total protease, high-alkaline trypsin (a trypsin subtype with highly alkaline pH optimum), low-alkaline trypsin (another trypsin subtype with slightly alkaline pH optimum), and chymotrypsin; TLCK inhibited the total protease and high-alkaline trypsin, whereas TPCK only activated the high-alkaline trypsin activities. STI had an inhibitory effect on all the proteases. These results showed that protease inhibitors had a certain extent inhibition to protease activities in the larval midgut of P. xylostella and that STI can potentially be used for effective pest control. The development of P. xylostella was delayed in the presence of different inhibitors. These effects were also related to the concentration of the inhibitor. A higher STI concentration showed a longer lasting effect but lower effect in this study compared to that of TLCK. The protease inhibitors had some inhibitory effect on the synthesis and secretion of proteases, and interfered with the protease activity, thereby inhibiting the absorption of nutrients and delaying the growth and development of P. xylostella and reducing their ability to reproduce. These findings should provide the baseline information about using for effective pest management in the future.https://www.frontiersin.org/article/10.3389/fphys.2018.01963/fullPlutella xylostellaprotease activityprotease inhibitors and activatorsgrowth and developmentmidgut
collection DOAJ
language English
format Article
sources DOAJ
author Aiping Zhao
Aiping Zhao
Yin Li
Yin Li
Chunmeng Leng
Chunmeng Leng
Ping Wang
Yiping Li
Yiping Li
spellingShingle Aiping Zhao
Aiping Zhao
Yin Li
Yin Li
Chunmeng Leng
Chunmeng Leng
Ping Wang
Yiping Li
Yiping Li
Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)
Frontiers in Physiology
Plutella xylostella
protease activity
protease inhibitors and activators
growth and development
midgut
author_facet Aiping Zhao
Aiping Zhao
Yin Li
Yin Li
Chunmeng Leng
Chunmeng Leng
Ping Wang
Yiping Li
Yiping Li
author_sort Aiping Zhao
title Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)
title_short Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)
title_full Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)
title_fullStr Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)
title_full_unstemmed Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)
title_sort inhibitory effect of protease inhibitors on larval midgut protease activities and the performance of plutella xylostella (lepidoptera: plutellidae)
publisher Frontiers Media S.A.
series Frontiers in Physiology
issn 1664-042X
publishDate 2019-01-01
description Plutella xylostella L. (diamondback moth) is a pest of cruciferous plants. To understand the relationship among protease inhibitors, protease activities and the growth and development of this insect, the activities of midgut proteases of P. xylostella larvae were determined in this study. Protease samples were extracted from the midguts of P. xylostella larvae, and the protease activities were determined using enzyme specific substrates. The results showed that CaCl2, EDTA, and EGTA inhibited only the trypsin. Among the common protease inhibitors, phenylmethyl sulfonyl fluorine (PMSF), Nα-p-methyl sulfonyl-L-lysine chloromethylketone (TLCK), Nα-methyl sulfonyl-L- phenylalanine chloromethyl ketone (TPCK), soybean trypsin inhibitor (STI), and PMSF inhibited the total protease, high-alkaline trypsin (a trypsin subtype with highly alkaline pH optimum), low-alkaline trypsin (another trypsin subtype with slightly alkaline pH optimum), and chymotrypsin; TLCK inhibited the total protease and high-alkaline trypsin, whereas TPCK only activated the high-alkaline trypsin activities. STI had an inhibitory effect on all the proteases. These results showed that protease inhibitors had a certain extent inhibition to protease activities in the larval midgut of P. xylostella and that STI can potentially be used for effective pest control. The development of P. xylostella was delayed in the presence of different inhibitors. These effects were also related to the concentration of the inhibitor. A higher STI concentration showed a longer lasting effect but lower effect in this study compared to that of TLCK. The protease inhibitors had some inhibitory effect on the synthesis and secretion of proteases, and interfered with the protease activity, thereby inhibiting the absorption of nutrients and delaying the growth and development of P. xylostella and reducing their ability to reproduce. These findings should provide the baseline information about using for effective pest management in the future.
topic Plutella xylostella
protease activity
protease inhibitors and activators
growth and development
midgut
url https://www.frontiersin.org/article/10.3389/fphys.2018.01963/full
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