Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans

Detalhes bibliográficos
Autor(a) principal: Amino, Rogerio [UNIFESP]
Data de Publicação: 1998
Outros Autores: Marques-Porto, Rafael [UNIFESP], Chammas, Roger [UNIFESP], Egami, Mizue Imoto [UNIFESP], Schenkman, Sergio [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://dx.doi.org/10.1074/jbc.273.38.24575
http://repositorio.unifesp.br/handle/11600/25959
Resumo: Sialidases (EC 3.2.1.18) are commonly found in viruses, bacteria, fungi, protozoa, and vertebrates, but not in invertebrates. We have previously reported the presence of a new siaIidase activity in the gut of exclusively hematophagous insects of the Triatoma genus, which transmit Chagas' disease (Amino, R., Acosta, A, Morita, O. M., Chioccola, V. L. P., and Schenkman, S. (1995) Glycobiology 5, 625-631). Here we show that this sialidase is present in the salivary gland of Triatoma infestans, and it is released with the saliva during the insect bite. the sialidase was purified to homogeneity (>5000 times) to a specific activity of more than 20 units/mg. It elutes from a gel filtration column with a volume corresponding to the size of 33 kDa, and it migrates as a single 26-kDa band in SDS-polyacrylamide gel electrophoresis, which is unusually smaller when compared with other known sialidases. T. infestans sialidase hydrolyzes preferentially alpha 2-->3-linked sialic acids at pH 4-8, with maximaI activity between pH 5.5 and 6.5, which is compatible with the optimal pH of secreted sialidases. the sialidase is competitively inhibited by 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid (K-i = 0.075 mM) and differently from many sialidases, with exception of Salmonella typhimurium sialidase, it is inhibited competitively by HEPES (K-i = 15 mM). the fact that T. infestans sialidase is released with the saliva and can hydrolyze sialyl-Lewis(x) blood groups, which are the ligands for selectins, suggests that it might have a role in the blood feeding.
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spelling Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestansSialidases (EC 3.2.1.18) are commonly found in viruses, bacteria, fungi, protozoa, and vertebrates, but not in invertebrates. We have previously reported the presence of a new siaIidase activity in the gut of exclusively hematophagous insects of the Triatoma genus, which transmit Chagas' disease (Amino, R., Acosta, A, Morita, O. M., Chioccola, V. L. P., and Schenkman, S. (1995) Glycobiology 5, 625-631). Here we show that this sialidase is present in the salivary gland of Triatoma infestans, and it is released with the saliva during the insect bite. the sialidase was purified to homogeneity (>5000 times) to a specific activity of more than 20 units/mg. It elutes from a gel filtration column with a volume corresponding to the size of 33 kDa, and it migrates as a single 26-kDa band in SDS-polyacrylamide gel electrophoresis, which is unusually smaller when compared with other known sialidases. T. infestans sialidase hydrolyzes preferentially alpha 2-->3-linked sialic acids at pH 4-8, with maximaI activity between pH 5.5 and 6.5, which is compatible with the optimal pH of secreted sialidases. the sialidase is competitively inhibited by 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid (K-i = 0.075 mM) and differently from many sialidases, with exception of Salmonella typhimurium sialidase, it is inhibited competitively by HEPES (K-i = 15 mM). the fact that T. infestans sialidase is released with the saliva and can hydrolyze sialyl-Lewis(x) blood groups, which are the ligands for selectins, suggests that it might have a role in the blood feeding.Universidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Histol, BR-04023062 São Paulo, BrazilLudwig Inst Canc Res, BR-01509010 São Paulo, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Histol, BR-04023062 São Paulo, BrazilWeb of ScienceAmer Soc Biochemistry Molecular Biology IncUniversidade Federal de São Paulo (UNIFESP)Ludwig Inst Canc ResAmino, Rogerio [UNIFESP]Marques-Porto, Rafael [UNIFESP]Chammas, Roger [UNIFESP]Egami, Mizue Imoto [UNIFESP]Schenkman, Sergio [UNIFESP]2016-01-24T12:30:40Z2016-01-24T12:30:40Z1998-09-18info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion24575-24582http://dx.doi.org/10.1074/jbc.273.38.24575Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 273, n. 38, p. 24575-24582, 1998.10.1074/jbc.273.38.245750021-9258http://repositorio.unifesp.br/handle/11600/25959WOS:000076007300044engJournal of Biological Chemistryinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2023-01-12T21:52:29Zoai:repositorio.unifesp.br/:11600/25959Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652023-01-12T21:52:29Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
title Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
spellingShingle Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
Amino, Rogerio [UNIFESP]
title_short Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
title_full Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
title_fullStr Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
title_full_unstemmed Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
title_sort Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
author Amino, Rogerio [UNIFESP]
author_facet Amino, Rogerio [UNIFESP]
Marques-Porto, Rafael [UNIFESP]
Chammas, Roger [UNIFESP]
Egami, Mizue Imoto [UNIFESP]
Schenkman, Sergio [UNIFESP]
author_role author
author2 Marques-Porto, Rafael [UNIFESP]
Chammas, Roger [UNIFESP]
Egami, Mizue Imoto [UNIFESP]
Schenkman, Sergio [UNIFESP]
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de São Paulo (UNIFESP)
Ludwig Inst Canc Res
dc.contributor.author.fl_str_mv Amino, Rogerio [UNIFESP]
Marques-Porto, Rafael [UNIFESP]
Chammas, Roger [UNIFESP]
Egami, Mizue Imoto [UNIFESP]
Schenkman, Sergio [UNIFESP]
description Sialidases (EC 3.2.1.18) are commonly found in viruses, bacteria, fungi, protozoa, and vertebrates, but not in invertebrates. We have previously reported the presence of a new siaIidase activity in the gut of exclusively hematophagous insects of the Triatoma genus, which transmit Chagas' disease (Amino, R., Acosta, A, Morita, O. M., Chioccola, V. L. P., and Schenkman, S. (1995) Glycobiology 5, 625-631). Here we show that this sialidase is present in the salivary gland of Triatoma infestans, and it is released with the saliva during the insect bite. the sialidase was purified to homogeneity (>5000 times) to a specific activity of more than 20 units/mg. It elutes from a gel filtration column with a volume corresponding to the size of 33 kDa, and it migrates as a single 26-kDa band in SDS-polyacrylamide gel electrophoresis, which is unusually smaller when compared with other known sialidases. T. infestans sialidase hydrolyzes preferentially alpha 2-->3-linked sialic acids at pH 4-8, with maximaI activity between pH 5.5 and 6.5, which is compatible with the optimal pH of secreted sialidases. the sialidase is competitively inhibited by 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid (K-i = 0.075 mM) and differently from many sialidases, with exception of Salmonella typhimurium sialidase, it is inhibited competitively by HEPES (K-i = 15 mM). the fact that T. infestans sialidase is released with the saliva and can hydrolyze sialyl-Lewis(x) blood groups, which are the ligands for selectins, suggests that it might have a role in the blood feeding.
publishDate 1998
dc.date.none.fl_str_mv 1998-09-18
2016-01-24T12:30:40Z
2016-01-24T12:30:40Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1074/jbc.273.38.24575
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 273, n. 38, p. 24575-24582, 1998.
10.1074/jbc.273.38.24575
0021-9258
http://repositorio.unifesp.br/handle/11600/25959
WOS:000076007300044
url http://dx.doi.org/10.1074/jbc.273.38.24575
http://repositorio.unifesp.br/handle/11600/25959
identifier_str_mv Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 273, n. 38, p. 24575-24582, 1998.
10.1074/jbc.273.38.24575
0021-9258
WOS:000076007300044
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of Biological Chemistry
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 24575-24582
dc.publisher.none.fl_str_mv Amer Soc Biochemistry Molecular Biology Inc
publisher.none.fl_str_mv Amer Soc Biochemistry Molecular Biology Inc
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
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