Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis
Autor(a) principal: | |
---|---|
Data de Publicação: | 2013 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | http://dx.doi.org/10.1007/s00360-013-0744-5 http://www.locus.ufv.br/handle/123456789/18842 |
Resumo: | The development of proteinase inhibitors as potential insect control agents has been constrained by insect adaptation to these compounds. The velvet bean caterpillar (Anticarsia gemmatalis) is a key soybean pest species that is well-adapted to proteinase inhibitors, particularly serine-proteinase inhibitors, which are abundant in the caterpillar host. The expression of diverse proteolytic enzymes by gut symbionts may allow the velvet bean caterpillar to circumvent proteinase inhibitors produced by the host plant. In this study, we characterized the proteolytic activity of the four nonpathogenic species of gut bacteria isolated from the velvet bean caterpillar—Bacillus cereus, Enterococcus gallinarum, Enterococcus mundtii and Staphylococcus xylosus. Two proteinase substrates, N-a-benzoyl- L -Arg-p-nitroanilide ( L -BApNA) and N-a-p-tosyl- L -Arg methyl ester ( L -TAME) and five proteinase inhibitors [aprotinin, E-64, ethylenediamine tetraacetic acid (EDTA), pepstatin and N-a-tosyl- L -lysine chloromethyl ketone (TLCK)] as well as CaCl 2 , pH and temperature profiles were used to characterize the expressed proteolytic activity of these bacterial strains in vitro. Kinetic parameters for proteolytic activity were also estimated. The results of these experiments indicated that serine- and cysteine-proteinase activities were expressed by all four gut bacteria symbionts of the velvet bean caterpillar. The cysteine- and serine-proteinase activities of these gut symbionts were distinct and different from that of gut proteinases of the caterpillar itself. This finding provides support for the potential involvement of gut symbionts in the mitigation of the negative effects of serine-proteinase inhibitors in the velvet bean caterpillar. |
id |
UFV_f94c624f75df0c604c4654b9d97d6ebd |
---|---|
oai_identifier_str |
oai:locus.ufv.br:123456789/18842 |
network_acronym_str |
UFV |
network_name_str |
LOCUS Repositório Institucional da UFV |
repository_id_str |
2145 |
spelling |
Pilon, F. M.Visôtto, L. E.Guedes, R. N. C.Oliveira, M. G. A.2018-04-19T13:57:58Z2018-04-19T13:57:58Z2013-02-081432136Xhttp://dx.doi.org/10.1007/s00360-013-0744-5http://www.locus.ufv.br/handle/123456789/18842The development of proteinase inhibitors as potential insect control agents has been constrained by insect adaptation to these compounds. The velvet bean caterpillar (Anticarsia gemmatalis) is a key soybean pest species that is well-adapted to proteinase inhibitors, particularly serine-proteinase inhibitors, which are abundant in the caterpillar host. The expression of diverse proteolytic enzymes by gut symbionts may allow the velvet bean caterpillar to circumvent proteinase inhibitors produced by the host plant. In this study, we characterized the proteolytic activity of the four nonpathogenic species of gut bacteria isolated from the velvet bean caterpillar—Bacillus cereus, Enterococcus gallinarum, Enterococcus mundtii and Staphylococcus xylosus. Two proteinase substrates, N-a-benzoyl- L -Arg-p-nitroanilide ( L -BApNA) and N-a-p-tosyl- L -Arg methyl ester ( L -TAME) and five proteinase inhibitors [aprotinin, E-64, ethylenediamine tetraacetic acid (EDTA), pepstatin and N-a-tosyl- L -lysine chloromethyl ketone (TLCK)] as well as CaCl 2 , pH and temperature profiles were used to characterize the expressed proteolytic activity of these bacterial strains in vitro. Kinetic parameters for proteolytic activity were also estimated. The results of these experiments indicated that serine- and cysteine-proteinase activities were expressed by all four gut bacteria symbionts of the velvet bean caterpillar. The cysteine- and serine-proteinase activities of these gut symbionts were distinct and different from that of gut proteinases of the caterpillar itself. This finding provides support for the potential involvement of gut symbionts in the mitigation of the negative effects of serine-proteinase inhibitors in the velvet bean caterpillar.engJournal of Comparative Physiology Bv. 183, n. 6, p. 735–747, Agosto 2013Springer-Verlag Berlin Heidelberginfo:eu-repo/semantics/openAccessGut microbiotaBacteria symbiontsBacteria–insect non-pathogenic interactionProteinaseProteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalisinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdftexto completoapplication/pdf761712https://locus.ufv.br//bitstream/123456789/18842/1/artigo.pdf7fb0dea3923a93b1155d4fb89c5120a0MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/18842/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILartigo.pdf.jpgartigo.pdf.jpgIM Thumbnailimage/jpeg5098https://locus.ufv.br//bitstream/123456789/18842/3/artigo.pdf.jpg13e118b192ef95cc7393be7e19af7d5aMD53123456789/188422018-04-19 23:01:02.084oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-04-20T02:01:02LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis |
title |
Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis |
spellingShingle |
Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis Pilon, F. M. Gut microbiota Bacteria symbionts Bacteria–insect non-pathogenic interaction Proteinase |
title_short |
Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis |
title_full |
Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis |
title_fullStr |
Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis |
title_full_unstemmed |
Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis |
title_sort |
Proteolytic activity of gut bacteria isolated from the velvet bean caterpillar Anticarsia gemmatalis |
author |
Pilon, F. M. |
author_facet |
Pilon, F. M. Visôtto, L. E. Guedes, R. N. C. Oliveira, M. G. A. |
author_role |
author |
author2 |
Visôtto, L. E. Guedes, R. N. C. Oliveira, M. G. A. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Pilon, F. M. Visôtto, L. E. Guedes, R. N. C. Oliveira, M. G. A. |
dc.subject.pt-BR.fl_str_mv |
Gut microbiota Bacteria symbionts Bacteria–insect non-pathogenic interaction Proteinase |
topic |
Gut microbiota Bacteria symbionts Bacteria–insect non-pathogenic interaction Proteinase |
description |
The development of proteinase inhibitors as potential insect control agents has been constrained by insect adaptation to these compounds. The velvet bean caterpillar (Anticarsia gemmatalis) is a key soybean pest species that is well-adapted to proteinase inhibitors, particularly serine-proteinase inhibitors, which are abundant in the caterpillar host. The expression of diverse proteolytic enzymes by gut symbionts may allow the velvet bean caterpillar to circumvent proteinase inhibitors produced by the host plant. In this study, we characterized the proteolytic activity of the four nonpathogenic species of gut bacteria isolated from the velvet bean caterpillar—Bacillus cereus, Enterococcus gallinarum, Enterococcus mundtii and Staphylococcus xylosus. Two proteinase substrates, N-a-benzoyl- L -Arg-p-nitroanilide ( L -BApNA) and N-a-p-tosyl- L -Arg methyl ester ( L -TAME) and five proteinase inhibitors [aprotinin, E-64, ethylenediamine tetraacetic acid (EDTA), pepstatin and N-a-tosyl- L -lysine chloromethyl ketone (TLCK)] as well as CaCl 2 , pH and temperature profiles were used to characterize the expressed proteolytic activity of these bacterial strains in vitro. Kinetic parameters for proteolytic activity were also estimated. The results of these experiments indicated that serine- and cysteine-proteinase activities were expressed by all four gut bacteria symbionts of the velvet bean caterpillar. The cysteine- and serine-proteinase activities of these gut symbionts were distinct and different from that of gut proteinases of the caterpillar itself. This finding provides support for the potential involvement of gut symbionts in the mitigation of the negative effects of serine-proteinase inhibitors in the velvet bean caterpillar. |
publishDate |
2013 |
dc.date.issued.fl_str_mv |
2013-02-08 |
dc.date.accessioned.fl_str_mv |
2018-04-19T13:57:58Z |
dc.date.available.fl_str_mv |
2018-04-19T13:57:58Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1007/s00360-013-0744-5 http://www.locus.ufv.br/handle/123456789/18842 |
dc.identifier.issn.none.fl_str_mv |
1432136X |
identifier_str_mv |
1432136X |
url |
http://dx.doi.org/10.1007/s00360-013-0744-5 http://www.locus.ufv.br/handle/123456789/18842 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
v. 183, n. 6, p. 735–747, Agosto 2013 |
dc.rights.driver.fl_str_mv |
Springer-Verlag Berlin Heidelberg info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Springer-Verlag Berlin Heidelberg |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Journal of Comparative Physiology B |
publisher.none.fl_str_mv |
Journal of Comparative Physiology B |
dc.source.none.fl_str_mv |
reponame:LOCUS Repositório Institucional da UFV instname:Universidade Federal de Viçosa (UFV) instacron:UFV |
instname_str |
Universidade Federal de Viçosa (UFV) |
instacron_str |
UFV |
institution |
UFV |
reponame_str |
LOCUS Repositório Institucional da UFV |
collection |
LOCUS Repositório Institucional da UFV |
bitstream.url.fl_str_mv |
https://locus.ufv.br//bitstream/123456789/18842/1/artigo.pdf https://locus.ufv.br//bitstream/123456789/18842/2/license.txt https://locus.ufv.br//bitstream/123456789/18842/3/artigo.pdf.jpg |
bitstream.checksum.fl_str_mv |
7fb0dea3923a93b1155d4fb89c5120a0 8a4605be74aa9ea9d79846c1fba20a33 13e118b192ef95cc7393be7e19af7d5a |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 |
repository.name.fl_str_mv |
LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV) |
repository.mail.fl_str_mv |
fabiojreis@ufv.br |
_version_ |
1801213032390459392 |