Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
Autor(a) principal: | |
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Data de Publicação: | 1998 |
Outros Autores: | , , , |
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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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 |
_version_ |
1814268274397937664 |