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Article: Interaction of human lung surfactant proteins A and D with mite (Dermatophagoides pteronyssinus) allergens

TitleInteraction of human lung surfactant proteins A and D with mite (Dermatophagoides pteronyssinus) allergens
Authors
KeywordsIgE
mite allergen
surfactant protein A
surfactant protein D
Issue Date1996
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/CEI
Citation
Clinical And Experimental Immunology, 1996, v. 106 n. 2, p. 367-373 How to Cite?
AbstractHuman lung surfactant proteins A (SP-A) and D (SP-D) are both collagenous C-type lectins which appear to mediate antimicrobial activity by binding to carbohydrates on micro-organisms and to receptors on phagocytic cells. Purified native SP-A and SP-D, isolated from human bronchoalveolar lavage fluid, were found to bind to whole mite extracts (Dermatophagoides pteronyssinus) and the purified allergen Der p I, in a carbohydrate-specific and calcium-dependent manner. Binding was inhibited by ethylenediamine tetra-acetic acid (EDTA) as well as by maltose in the case of SP-D, or mannose in the case of SP-A. A recombinant polypeptide, which trimerized to form the neck region and carbohydrate recognition domains of SP-D, also inhibited the binding of native SP-D to the whole mite extract and Der p I. Both SP-A and SP-D did not bind to deglycosylated whole mite extracts or to recombinant Der p proteins, which lacked carbohydrate residues. These results suggest that the ability of surfactant proteins to bind certain allergens is mediated through their carbohydrate-recognition domains (CRDs) interacting with carbohydrate residues on the allergens. Moreover, SP-A and SP-D were found to inhibit allergen-specific IgE binding to the mite extracts either via steric hindrance or competitive binding. It is therefore possible that SP-A and SP-D may be involved in the modulation of allergen sensitization and/or the development of allergic reactions.
Persistent Identifierhttp://hdl.handle.net/10722/49432
ISSN
2015 Impact Factor: 3.148
2015 SCImago Journal Rankings: 1.369
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, JYen_HK
dc.contributor.authorKishore, Uen_HK
dc.contributor.authorLim, BLen_HK
dc.contributor.authorStrong, Pen_HK
dc.contributor.authorReid, KBMen_HK
dc.date.accessioned2008-06-12T06:42:31Z-
dc.date.available2008-06-12T06:42:31Z-
dc.date.issued1996en_HK
dc.identifier.citationClinical And Experimental Immunology, 1996, v. 106 n. 2, p. 367-373en_HK
dc.identifier.issn0009-9104en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49432-
dc.description.abstractHuman lung surfactant proteins A (SP-A) and D (SP-D) are both collagenous C-type lectins which appear to mediate antimicrobial activity by binding to carbohydrates on micro-organisms and to receptors on phagocytic cells. Purified native SP-A and SP-D, isolated from human bronchoalveolar lavage fluid, were found to bind to whole mite extracts (Dermatophagoides pteronyssinus) and the purified allergen Der p I, in a carbohydrate-specific and calcium-dependent manner. Binding was inhibited by ethylenediamine tetra-acetic acid (EDTA) as well as by maltose in the case of SP-D, or mannose in the case of SP-A. A recombinant polypeptide, which trimerized to form the neck region and carbohydrate recognition domains of SP-D, also inhibited the binding of native SP-D to the whole mite extract and Der p I. Both SP-A and SP-D did not bind to deglycosylated whole mite extracts or to recombinant Der p proteins, which lacked carbohydrate residues. These results suggest that the ability of surfactant proteins to bind certain allergens is mediated through their carbohydrate-recognition domains (CRDs) interacting with carbohydrate residues on the allergens. Moreover, SP-A and SP-D were found to inhibit allergen-specific IgE binding to the mite extracts either via steric hindrance or competitive binding. It is therefore possible that SP-A and SP-D may be involved in the modulation of allergen sensitization and/or the development of allergic reactions.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/CEIen_HK
dc.relation.ispartofClinical and Experimental Immunologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsClinical and Experimental Immunology. Copyright © Blackwell Publishing Ltd.en_HK
dc.rightsThe definitive version is available at www.blackwell-synergy.comen_HK
dc.subjectIgEen_HK
dc.subjectmite allergenen_HK
dc.subjectsurfactant protein Aen_HK
dc.subjectsurfactant protein Den_HK
dc.titleInteraction of human lung surfactant proteins A and D with mite (Dermatophagoides pteronyssinus) allergensen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0009-9104&volume=106&issue=2&spage=367&epage=373&date=1996&atitle=Interaction+of+human+lung+surfactant+proteins+A+and+D+with+mite+(Dermatophagoides+pteronyssinus)+allergensen_HK
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_HK
dc.identifier.authorityLim, BL=rp00744en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1046/j.1365-2249.1996.d01-838.xen_HK
dc.identifier.pmid8918587en_HK
dc.identifier.pmcidPMC2200585-
dc.identifier.scopuseid_2-s2.0-0029822715en_HK
dc.identifier.hkuros24511-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029822715&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume106en_HK
dc.identifier.issue2en_HK
dc.identifier.spage367en_HK
dc.identifier.epage373en_HK
dc.identifier.isiWOS:A1996VQ33800027-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWang, JY=8089862700en_HK
dc.identifier.scopusauthoridKishore, U=7003804532en_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK
dc.identifier.scopusauthoridStrong, P=7101900796en_HK
dc.identifier.scopusauthoridReid, KBM=7202780648en_HK

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