A role for human Sp alpha as a pattern-recognition receptor

Human Sp alpha is a soluble protein belonging to group B of the scavenger receptor cysteine-rich (SRCR) superfamily for which little functional information is available. It is expressed by macrophages present in lymphoid tissues (spleen, lymph node, thymus, and bone marrow), and it binds to myelomon...

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Autores: Sarrias Fornés, Maria Rosa, Roselló, Sandra, Sánchez-Barbero, Fernando, Sierra Ortigosa, Josep Maria, Vila Estapé, Jordi, Yélamos, José, Vives, Jordi, Casals, Cristina, Lozano Soto, Francisco
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2005
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/176948
Acceso en línea:https://hdl.handle.net/2445/176948
Access Level:acceso abierto
Palabra clave:Receptors cel·lulars
Immunologia
Fisiologia
Cell receptors
Immunology
Physiology
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spelling A role for human Sp alpha as a pattern-recognition receptorSarrias Fornés, Maria RosaRoselló, SandraSánchez-Barbero, FernandoSierra Ortigosa, Josep MariaVila Estapé, JordiYélamos, JoséVives, JordiCasals, CristinaLozano Soto, FranciscoReceptors cel·lularsImmunologiaFisiologiaCell receptorsImmunologyPhysiologyHuman Sp alpha is a soluble protein belonging to group B of the scavenger receptor cysteine-rich (SRCR) superfamily for which little functional information is available. It is expressed by macrophages present in lymphoid tissues (spleen, lymph node, thymus, and bone marrow), and it binds to myelomonocytic and lymphoid cells, which suggests that it may play an important role in the regulation of the innate and adaptive immune systems. In the present study we show that recombinant human Sp alpha (rSp alpha) binds to the surface of several gram-positive and gram-negative bacterial strains. Competition studies indicated that such binding is mediated by the recognition of lipoteichoic acid (LTA) and lipopolysaccharide (LPS), respectively, through nonoverlapping sites on the Sp alpha molecule. The most conserved part of LPS (2-keto-3-deoxyoctulosonic acid and lipid A) was shown to be involved in the recognition by Sp alpha. Bacterial binding studies using the SRCR domain 1 of Sp alpha showed that this domain retains both the LPS and LTA binding activities, indicating that both bacterial interacting sites are retained in a single SRCR domain. Furthermore, rSp alpha induced aggregation of gram-positive and gram-negative bacteria strains. On the other hand, rSp alpha inhibited tumor necrosis factor-alpha secretion by human monocytes stimulated with LPS or LTA. Binding of Sp alpha to conserved components of bacterial surfaces and modulation of the monocyte response indicate that this molecule is an active constituent of the innate immune response of the host.American Society for Biochemistry and Molecular Biology2005info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/176948Articles publicats en revistes (Patologia i Terapèutica Experimental)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.1074/jbc.M505042200Journal of Biological Chemistry, 2005, vol. 280, num. 42, p. 35391-35398https://doi.org/10.1074/jbc.M505042200(c) American Society for Biochemistry and Molecular Biology, 2005info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1769482026-05-27T06:46:51Z
dc.title.none.fl_str_mv A role for human Sp alpha as a pattern-recognition receptor
title A role for human Sp alpha as a pattern-recognition receptor
spellingShingle A role for human Sp alpha as a pattern-recognition receptor
Sarrias Fornés, Maria Rosa
Receptors cel·lulars
Immunologia
Fisiologia
Cell receptors
Immunology
Physiology
title_short A role for human Sp alpha as a pattern-recognition receptor
title_full A role for human Sp alpha as a pattern-recognition receptor
title_fullStr A role for human Sp alpha as a pattern-recognition receptor
title_full_unstemmed A role for human Sp alpha as a pattern-recognition receptor
title_sort A role for human Sp alpha as a pattern-recognition receptor
dc.creator.none.fl_str_mv Sarrias Fornés, Maria Rosa
Roselló, Sandra
Sánchez-Barbero, Fernando
Sierra Ortigosa, Josep Maria
Vila Estapé, Jordi
Yélamos, José
Vives, Jordi
Casals, Cristina
Lozano Soto, Francisco
author Sarrias Fornés, Maria Rosa
author_facet Sarrias Fornés, Maria Rosa
Roselló, Sandra
Sánchez-Barbero, Fernando
Sierra Ortigosa, Josep Maria
Vila Estapé, Jordi
Yélamos, José
Vives, Jordi
Casals, Cristina
Lozano Soto, Francisco
author_role author
author2 Roselló, Sandra
Sánchez-Barbero, Fernando
Sierra Ortigosa, Josep Maria
Vila Estapé, Jordi
Yélamos, José
Vives, Jordi
Casals, Cristina
Lozano Soto, Francisco
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Receptors cel·lulars
Immunologia
Fisiologia
Cell receptors
Immunology
Physiology
topic Receptors cel·lulars
Immunologia
Fisiologia
Cell receptors
Immunology
Physiology
description Human Sp alpha is a soluble protein belonging to group B of the scavenger receptor cysteine-rich (SRCR) superfamily for which little functional information is available. It is expressed by macrophages present in lymphoid tissues (spleen, lymph node, thymus, and bone marrow), and it binds to myelomonocytic and lymphoid cells, which suggests that it may play an important role in the regulation of the innate and adaptive immune systems. In the present study we show that recombinant human Sp alpha (rSp alpha) binds to the surface of several gram-positive and gram-negative bacterial strains. Competition studies indicated that such binding is mediated by the recognition of lipoteichoic acid (LTA) and lipopolysaccharide (LPS), respectively, through nonoverlapping sites on the Sp alpha molecule. The most conserved part of LPS (2-keto-3-deoxyoctulosonic acid and lipid A) was shown to be involved in the recognition by Sp alpha. Bacterial binding studies using the SRCR domain 1 of Sp alpha showed that this domain retains both the LPS and LTA binding activities, indicating that both bacterial interacting sites are retained in a single SRCR domain. Furthermore, rSp alpha induced aggregation of gram-positive and gram-negative bacteria strains. On the other hand, rSp alpha inhibited tumor necrosis factor-alpha secretion by human monocytes stimulated with LPS or LTA. Binding of Sp alpha to conserved components of bacterial surfaces and modulation of the monocyte response indicate that this molecule is an active constituent of the innate immune response of the host.
publishDate 2005
dc.date.none.fl_str_mv 2005
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/176948
url https://hdl.handle.net/2445/176948
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1074/jbc.M505042200
Journal of Biological Chemistry, 2005, vol. 280, num. 42, p. 35391-35398
https://doi.org/10.1074/jbc.M505042200
dc.rights.none.fl_str_mv (c) American Society for Biochemistry and Molecular Biology, 2005
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) American Society for Biochemistry and Molecular Biology, 2005
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv Articles publicats en revistes (Patologia i Terapèutica Experimental)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300724

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