Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells

Detalhes bibliográficos
Autor(a) principal: Plotkowski, M. C.
Data de Publicação: 2001
Outros Autores: Costa, A. O., Morandi, V, Barbosa, H. S., Nader, Helena Bonciani [UNIFESP], De Bentzmann, S., Puchelle, E.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://dx.doi.org/10.1099/0022-1317-50-2-183
http://repositorio.unifesp.br/handle/11600/44504
Resumo: Tight junctions seal polarised surface epithelial respiratory cells so as to prevent the passage of bacteria and toxins through the epithelial sheet. Disruption of tight junctions, which may occur during injury and repair processes of airway epithelium, favours potential bacterial interaction with receptors from cell basolateral membranes. Earlier studies reported that non-polarised and untight epithelial respiratory cells are highly susceptible to Pseudomonas aeruginosa adherence and internalisation, As heparan sulphate proteoglycans (HSP) from cell basolateral membranes in epithelial cells without tight junctions may become accessible to bacterial ligands, the present study investigated their role as potential receptors for non-piliate P. aeruginosa ligands, Treatment of cells with heparitinase I and II significantly reduced (51.2% and 51.7%, respectively) P. aeruginosa adherence to epithelial respiratory cells without tight junctions, The internalisation of bacteria was not affected by treatment,vith heparitinases, Treatment of the bacteria with heparin and heparan sulphate also significantly reduced their adherence to respiratory cells (34.3% and 43.7%, respectively). Treatment of cells with other enzymes (trypsin, lipase and chondroitinase ABC) or treatment of bacteria with chondroitin-4-sulphate did not modify the adherence to respiratory cells significantly. Both affinity chromatography and Western blotting assays showed the interaction of different P. aeruginosa outer-membrane proteins (OMPs) with heparin, Several bacterial strains showed differences in their profile of heparin-binding OMPs, but all exhibited low mol, wt (< 30 kDa) reactive proteins. Reactivity of whole bacterial cells with heparin was also observed by transmission electron microscopy, These results suggest that HSP are potential receptors for P. aeruginosa adherence to non-polarised and untight epithelial respiratory cells.
id UFSP_bf25c77924452a2daeb04fd4913e6e99
oai_identifier_str oai:repositorio.unifesp.br/:11600/44504
network_acronym_str UFSP
network_name_str Repositório Institucional da UNIFESP
repository_id_str 3465
spelling Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cellsTight junctions seal polarised surface epithelial respiratory cells so as to prevent the passage of bacteria and toxins through the epithelial sheet. Disruption of tight junctions, which may occur during injury and repair processes of airway epithelium, favours potential bacterial interaction with receptors from cell basolateral membranes. Earlier studies reported that non-polarised and untight epithelial respiratory cells are highly susceptible to Pseudomonas aeruginosa adherence and internalisation, As heparan sulphate proteoglycans (HSP) from cell basolateral membranes in epithelial cells without tight junctions may become accessible to bacterial ligands, the present study investigated their role as potential receptors for non-piliate P. aeruginosa ligands, Treatment of cells with heparitinase I and II significantly reduced (51.2% and 51.7%, respectively) P. aeruginosa adherence to epithelial respiratory cells without tight junctions, The internalisation of bacteria was not affected by treatment,vith heparitinases, Treatment of the bacteria with heparin and heparan sulphate also significantly reduced their adherence to respiratory cells (34.3% and 43.7%, respectively). Treatment of cells with other enzymes (trypsin, lipase and chondroitinase ABC) or treatment of bacteria with chondroitin-4-sulphate did not modify the adherence to respiratory cells significantly. Both affinity chromatography and Western blotting assays showed the interaction of different P. aeruginosa outer-membrane proteins (OMPs) with heparin, Several bacterial strains showed differences in their profile of heparin-binding OMPs, but all exhibited low mol, wt (< 30 kDa) reactive proteins. Reactivity of whole bacterial cells with heparin was also observed by transmission electron microscopy, These results suggest that HSP are potential receptors for P. aeruginosa adherence to non-polarised and untight epithelial respiratory cells.Univ Estado Rio de Janeiro, Dept Microbiol & Immunol, Rio De Janeiro, BrazilUniv Estado Rio de Janeiro, Dept Cell Biol & Genet, Rio De Janeiro, BrazilFIOCRUZ, Dept Ultrastruct & Cell Biol, BR-21045900 Rio De Janeiro, BrazilEscola Paulista Med, Dept Biochem, BR-04023 Sao Paulo, BrazilINSERM, U514, Reims, FranceEscola Paulista Med, Dept Biochem, BR-04023 Sao Paulo, BrazilWeb of ScienceLippincott Williams & WilkinsUniversidade do Estado do Rio de Janeiro (UERJ)FIOCRUZUniversidade Federal de São Paulo (UNIFESP)INSERMPlotkowski, M. C.Costa, A. O.Morandi, VBarbosa, H. S.Nader, Helena Bonciani [UNIFESP]De Bentzmann, S.Puchelle, E.2018-06-15T18:07:27Z2018-06-15T18:07:27Z2001-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion183-190http://dx.doi.org/10.1099/0022-1317-50-2-183Journal Of Medical Microbiology. Philadelphia: Lippincott Williams & Wilkins, v. 50, n. 2, p. 183-190, 2001.10.1099/0022-1317-50-2-1830022-2615http://repositorio.unifesp.br/handle/11600/44504WOS:000166649300011engJournal Of Medical Microbiologyinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-05-02T13:58:41Zoai:repositorio.unifesp.br/:11600/44504Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-05-02T13:58:41Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
title Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
spellingShingle Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
Plotkowski, M. C.
title_short Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
title_full Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
title_fullStr Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
title_full_unstemmed Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
title_sort Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
author Plotkowski, M. C.
author_facet Plotkowski, M. C.
Costa, A. O.
Morandi, V
Barbosa, H. S.
Nader, Helena Bonciani [UNIFESP]
De Bentzmann, S.
Puchelle, E.
author_role author
author2 Costa, A. O.
Morandi, V
Barbosa, H. S.
Nader, Helena Bonciani [UNIFESP]
De Bentzmann, S.
Puchelle, E.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Estado do Rio de Janeiro (UERJ)
FIOCRUZ
Universidade Federal de São Paulo (UNIFESP)
INSERM
dc.contributor.author.fl_str_mv Plotkowski, M. C.
Costa, A. O.
Morandi, V
Barbosa, H. S.
Nader, Helena Bonciani [UNIFESP]
De Bentzmann, S.
Puchelle, E.
description Tight junctions seal polarised surface epithelial respiratory cells so as to prevent the passage of bacteria and toxins through the epithelial sheet. Disruption of tight junctions, which may occur during injury and repair processes of airway epithelium, favours potential bacterial interaction with receptors from cell basolateral membranes. Earlier studies reported that non-polarised and untight epithelial respiratory cells are highly susceptible to Pseudomonas aeruginosa adherence and internalisation, As heparan sulphate proteoglycans (HSP) from cell basolateral membranes in epithelial cells without tight junctions may become accessible to bacterial ligands, the present study investigated their role as potential receptors for non-piliate P. aeruginosa ligands, Treatment of cells with heparitinase I and II significantly reduced (51.2% and 51.7%, respectively) P. aeruginosa adherence to epithelial respiratory cells without tight junctions, The internalisation of bacteria was not affected by treatment,vith heparitinases, Treatment of the bacteria with heparin and heparan sulphate also significantly reduced their adherence to respiratory cells (34.3% and 43.7%, respectively). Treatment of cells with other enzymes (trypsin, lipase and chondroitinase ABC) or treatment of bacteria with chondroitin-4-sulphate did not modify the adherence to respiratory cells significantly. Both affinity chromatography and Western blotting assays showed the interaction of different P. aeruginosa outer-membrane proteins (OMPs) with heparin, Several bacterial strains showed differences in their profile of heparin-binding OMPs, but all exhibited low mol, wt (< 30 kDa) reactive proteins. Reactivity of whole bacterial cells with heparin was also observed by transmission electron microscopy, These results suggest that HSP are potential receptors for P. aeruginosa adherence to non-polarised and untight epithelial respiratory cells.
publishDate 2001
dc.date.none.fl_str_mv 2001-02-01
2018-06-15T18:07:27Z
2018-06-15T18:07:27Z
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/10.1099/0022-1317-50-2-183
Journal Of Medical Microbiology. Philadelphia: Lippincott Williams & Wilkins, v. 50, n. 2, p. 183-190, 2001.
10.1099/0022-1317-50-2-183
0022-2615
http://repositorio.unifesp.br/handle/11600/44504
WOS:000166649300011
url http://dx.doi.org/10.1099/0022-1317-50-2-183
http://repositorio.unifesp.br/handle/11600/44504
identifier_str_mv Journal Of Medical Microbiology. Philadelphia: Lippincott Williams & Wilkins, v. 50, n. 2, p. 183-190, 2001.
10.1099/0022-1317-50-2-183
0022-2615
WOS:000166649300011
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal Of Medical Microbiology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 183-190
dc.publisher.none.fl_str_mv Lippincott Williams & Wilkins
publisher.none.fl_str_mv Lippincott Williams & Wilkins
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_ 1814268358020825088