2.50
Hdl Handle:
http://hdl.handle.net/10033/18872
Title:
Antibodies against C-reactive protein cross-react with 60-kilodalton heat shock proteins.
Authors:
Udvarnoki, Katalin; Cervenak, László; Uray, Katalin; Hudecz, Ferenc; Kacskovics, Imre; Spallek, Ralf; Singh, Mahavir; Füst, George; Prohászka, Zoltán
Abstract:
C-reactive protein (CRP) is an acute-phase reactant frequently used in histochemistry as a marker of ongoing inflammation. Furthermore, CRP is a powerful biomarker for the prediction of coronary artery disease risk. Heat-shock protein 60 (Hsp60) and CRP are complement-activating molecules, and the effect of their interactions on the regulation of complement activation was studied. However, during the first experiments, we learned that polyclonal anti-CRP antibodies cross-react with Hsp60. Therefore, the aim of our present study was to analyze the cross-reactivity of anti-CRP antibodies (Ab) with Hsp60 in solid-phase enzyme immune assays, in epitope studies using a series of overlapping synthetic peptides, and in Ouchterlony analyses. We found that three different commercial rabbit polyclonal antibodies and two monoclonal (9C9 and CRP-8) anti-CRP antibodies specifically recognize recombinant human Hsp60 and recombinant Mycobacterium tuberculosis Hsp65, respectively. Hsp60 was found to inhibit the binding of anti-CRP polyclonal Ab to Hsp60. Six epitope regions of Hsp60 were recognized by the anti-CRP antibodies, and one region (amino acids [AA] 218 to 232) was recognized by monoclonal antibodies CRP-8 and 9C9. This epitope region of Hsp60 displays 26.6% amino acid identity to CRP AA region 77 to 90. These data suggest that the B-cell epitopes shared between CRP and Hsp60 give rise to a true mimicry-based cross-reaction and the induction of cross-reactive antibodies. Our study underlines the importance of thorough study design and careful interpretation of results while using polyclonal anti-CRP antibodies for histochemistry, especially at low dilutions. Furthermore, analytical interference with Hsp60 in CRP assays should also be tested.
Affiliation:
Third Department of Medicine, Semmelweis University, H-1125 Budapest, Kútvölgyi st. 4, Hungary.
Citation:
Antibodies against C-reactive protein cross-react with 60-kilodalton heat shock proteins. 2007, 14 (4):335-41 Clin. Vaccine Immunol.
Journal:
Clinical and vaccine immunology : CVI
Issue Date:
Apr-2007
URI:
http://hdl.handle.net/10033/18872
DOI:
10.1128/CVI.00155-06
PubMed ID:
17301219
Type:
Article
Language:
en
ISSN:
1556-6811
Appears in Collections:
Publications of Dept. Genome Analysis (GNA)

Full metadata record

DC FieldValue Language
dc.contributor.authorUdvarnoki, Katalin-
dc.contributor.authorCervenak, László-
dc.contributor.authorUray, Katalin-
dc.contributor.authorHudecz, Ferenc-
dc.contributor.authorKacskovics, Imre-
dc.contributor.authorSpallek, Ralf-
dc.contributor.authorSingh, Mahavir-
dc.contributor.authorFüst, George-
dc.contributor.authorProhászka, Zoltán-
dc.date.accessioned2008-02-21T14:09:36Z-
dc.date.available2008-02-21T14:09:36Z-
dc.date.issued2007-04-
dc.identifier.citationAntibodies against C-reactive protein cross-react with 60-kilodalton heat shock proteins. 2007, 14 (4):335-41 Clin. Vaccine Immunol.en
dc.identifier.issn1556-6811-
dc.identifier.pmid17301219-
dc.identifier.doi10.1128/CVI.00155-06-
dc.identifier.urihttp://hdl.handle.net/10033/18872-
dc.description.abstractC-reactive protein (CRP) is an acute-phase reactant frequently used in histochemistry as a marker of ongoing inflammation. Furthermore, CRP is a powerful biomarker for the prediction of coronary artery disease risk. Heat-shock protein 60 (Hsp60) and CRP are complement-activating molecules, and the effect of their interactions on the regulation of complement activation was studied. However, during the first experiments, we learned that polyclonal anti-CRP antibodies cross-react with Hsp60. Therefore, the aim of our present study was to analyze the cross-reactivity of anti-CRP antibodies (Ab) with Hsp60 in solid-phase enzyme immune assays, in epitope studies using a series of overlapping synthetic peptides, and in Ouchterlony analyses. We found that three different commercial rabbit polyclonal antibodies and two monoclonal (9C9 and CRP-8) anti-CRP antibodies specifically recognize recombinant human Hsp60 and recombinant Mycobacterium tuberculosis Hsp65, respectively. Hsp60 was found to inhibit the binding of anti-CRP polyclonal Ab to Hsp60. Six epitope regions of Hsp60 were recognized by the anti-CRP antibodies, and one region (amino acids [AA] 218 to 232) was recognized by monoclonal antibodies CRP-8 and 9C9. This epitope region of Hsp60 displays 26.6% amino acid identity to CRP AA region 77 to 90. These data suggest that the B-cell epitopes shared between CRP and Hsp60 give rise to a true mimicry-based cross-reaction and the induction of cross-reactive antibodies. Our study underlines the importance of thorough study design and careful interpretation of results while using polyclonal anti-CRP antibodies for histochemistry, especially at low dilutions. Furthermore, analytical interference with Hsp60 in CRP assays should also be tested.en
dc.language.isoenen
dc.subject.meshAnimalsen
dc.subject.meshAntibodiesen
dc.subject.meshBacterial Proteinsen
dc.subject.meshBinding Sites, Antibodyen
dc.subject.meshC-Reactive Proteinen
dc.subject.meshChaperonin 60en
dc.subject.meshChaperoninsen
dc.subject.meshCross Reactionsen
dc.subject.meshHumansen
dc.subject.meshMiceen
dc.subject.meshMycobacterium tuberculosisen
dc.subject.meshRabbitsen
dc.titleAntibodies against C-reactive protein cross-react with 60-kilodalton heat shock proteins.en
dc.typeArticleen
dc.contributor.departmentThird Department of Medicine, Semmelweis University, H-1125 Budapest, Kútvölgyi st. 4, Hungary.en
dc.identifier.journalClinical and vaccine immunology : CVIen

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