Identification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestans
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Publication Date: | 1998 |
Other Authors: | , , , |
Format: | Article |
Language: | eng |
Source: | Repositório Institucional da UNIFESP |
Download full: | http://repositorio.unifesp.br/handle/11600/25959 http://dx.doi.org/10.1074/jbc.273.38.24575 |
Summary: | 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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Amino, Rogerio [UNIFESP]Marques-Porto, Rafael [UNIFESP]Chammas, Roger [UNIFESP]Egami, Mizue Imoto [UNIFESP]Schenkman, Sergio [UNIFESP]Universidade Federal de São Paulo (UNIFESP)Ludwig Inst Canc Res2016-01-24T12:30:40Z2016-01-24T12:30:40Z1998-09-18Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 273, n. 38, p. 24575-24582, 1998.0021-9258http://repositorio.unifesp.br/handle/11600/25959http://dx.doi.org/10.1074/jbc.273.38.2457510.1074/jbc.273.38.24575WOS:000076007300044Sialidases (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 Science24575-24582engAmer Soc Biochemistry Molecular Biology IncJournal of Biological ChemistryIdentification and characterization of a sialidase released by the salivary gland of the hematophagous insect Triatoma infestansinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/259592023-01-12 21:52:29.058metadata only accessoai:repositorio.unifesp.br:11600/25959Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-25T12:10:21.636959Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.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.institution.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.issued.fl_str_mv |
1998-09-18 |
dc.date.accessioned.fl_str_mv |
2016-01-24T12:30:40Z |
dc.date.available.fl_str_mv |
2016-01-24T12:30:40Z |
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.citation.fl_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 273, n. 38, p. 24575-24582, 1998. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/25959 http://dx.doi.org/10.1074/jbc.273.38.24575 |
dc.identifier.issn.none.fl_str_mv |
0021-9258 |
dc.identifier.doi.none.fl_str_mv |
10.1074/jbc.273.38.24575 |
dc.identifier.wos.none.fl_str_mv |
WOS:000076007300044 |
identifier_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 273, n. 38, p. 24575-24582, 1998. 0021-9258 10.1074/jbc.273.38.24575 WOS:000076007300044 |
url |
http://repositorio.unifesp.br/handle/11600/25959 http://dx.doi.org/10.1074/jbc.273.38.24575 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.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) |
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UNIFESP |
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UNIFESP |
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Repositório Institucional da UNIFESP |
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Repositório Institucional da UNIFESP |
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Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
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1783460258683813888 |