Identification of streptococcal proteins reacting with sera from Behçet's disease and rheumatic disorders

Sung Bin Cho, JuHee Lee, Keun Jae Ahn, Suhyun Cho, YongBeom Park, Soo Kon Lee, Dongsik Bang, Kwanghoon Lee

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Objective. We evaluated the reactivity of sera from Behçet's disease (BD), systemic lupus erythematosus (SLE), dermatomyositis (DM), rheumatoid arthritis (RA), and Takayasu's arteritis (TA) patients against human α-enolase and streptococcal α-enolase, and identified additional streptococcal antigens. Methods. Enzyme-linked immunosorbent assay (ELISA) and immunoblotting were performed using sera from patients with BD, SLE, DM, RA, and TA and healthy volunteers (control) against human α-enolase and streptococcal α-enolase. Immunoblot analysis and matrix-assisted laser desorption ionisation-time-of-flight mass spectrometry were used to identify and recombine other streptococcal antigens. Results. Specific positive signals against recombinant human α-enolase were detected by IgM ELISA of serum samples from 50% of BD, 14.3% of SLE, 57.1% of DM, 42.9% of RA, and 57.1% of TA patients. Specific positive signals against streptococcal α-enolase were detected from 42.9% of BD, 14.3% of DM, and 14.3% of TA patients. No SLE and RA sera reacted against streptococcal a-enolase antigen. Streptococcal proteins reacting with sera were identified as hypothetical protein (HP) for SLE and DM patients, acid phosphatase (AP) for RA patients, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) for TA patients. Conclusions. We observed that RA patients did not present serum reactivity against either HP or GAPDH though BD, SLE, DM, and TA patients did. Also, AP reacted with sera from BD, SLE, DM, RA, and TA patients.

Original languageEnglish
JournalClinical and Experimental Rheumatology
Volume28
Issue number4 SUPPL. 60
Publication statusPublished - 2010 Jul 1

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Rheumatic Diseases
Takayasu Arteritis
Dermatomyositis
Phosphopyruvate Hydratase
Systemic Lupus Erythematosus
Rheumatoid Arthritis
Serum
Proteins
Glyceraldehyde-3-Phosphate Dehydrogenases
Acid Phosphatase
Antigens
Enzyme-Linked Immunosorbent Assay
Immunoblotting
Immunoglobulin M
Mass Spectrometry
Healthy Volunteers
Lasers

All Science Journal Classification (ASJC) codes

  • Rheumatology
  • Immunology and Allergy
  • Immunology

Cite this

@article{2239626fc9694be0bbc7916fc1572db3,
title = "Identification of streptococcal proteins reacting with sera from Beh{\cc}et's disease and rheumatic disorders",
abstract = "Objective. We evaluated the reactivity of sera from Beh{\cc}et's disease (BD), systemic lupus erythematosus (SLE), dermatomyositis (DM), rheumatoid arthritis (RA), and Takayasu's arteritis (TA) patients against human α-enolase and streptococcal α-enolase, and identified additional streptococcal antigens. Methods. Enzyme-linked immunosorbent assay (ELISA) and immunoblotting were performed using sera from patients with BD, SLE, DM, RA, and TA and healthy volunteers (control) against human α-enolase and streptococcal α-enolase. Immunoblot analysis and matrix-assisted laser desorption ionisation-time-of-flight mass spectrometry were used to identify and recombine other streptococcal antigens. Results. Specific positive signals against recombinant human α-enolase were detected by IgM ELISA of serum samples from 50{\%} of BD, 14.3{\%} of SLE, 57.1{\%} of DM, 42.9{\%} of RA, and 57.1{\%} of TA patients. Specific positive signals against streptococcal α-enolase were detected from 42.9{\%} of BD, 14.3{\%} of DM, and 14.3{\%} of TA patients. No SLE and RA sera reacted against streptococcal a-enolase antigen. Streptococcal proteins reacting with sera were identified as hypothetical protein (HP) for SLE and DM patients, acid phosphatase (AP) for RA patients, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) for TA patients. Conclusions. We observed that RA patients did not present serum reactivity against either HP or GAPDH though BD, SLE, DM, and TA patients did. Also, AP reacted with sera from BD, SLE, DM, RA, and TA patients.",
author = "Cho, {Sung Bin} and JuHee Lee and Ahn, {Keun Jae} and Suhyun Cho and YongBeom Park and Lee, {Soo Kon} and Dongsik Bang and Kwanghoon Lee",
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Identification of streptococcal proteins reacting with sera from Behçet's disease and rheumatic disorders. / Cho, Sung Bin; Lee, JuHee; Ahn, Keun Jae; Cho, Suhyun; Park, YongBeom; Lee, Soo Kon; Bang, Dongsik; Lee, Kwanghoon.

In: Clinical and Experimental Rheumatology, Vol. 28, No. 4 SUPPL. 60, 01.07.2010.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Identification of streptococcal proteins reacting with sera from Behçet's disease and rheumatic disorders

AU - Cho, Sung Bin

AU - Lee, JuHee

AU - Ahn, Keun Jae

AU - Cho, Suhyun

AU - Park, YongBeom

AU - Lee, Soo Kon

AU - Bang, Dongsik

AU - Lee, Kwanghoon

PY - 2010/7/1

Y1 - 2010/7/1

N2 - Objective. We evaluated the reactivity of sera from Behçet's disease (BD), systemic lupus erythematosus (SLE), dermatomyositis (DM), rheumatoid arthritis (RA), and Takayasu's arteritis (TA) patients against human α-enolase and streptococcal α-enolase, and identified additional streptococcal antigens. Methods. Enzyme-linked immunosorbent assay (ELISA) and immunoblotting were performed using sera from patients with BD, SLE, DM, RA, and TA and healthy volunteers (control) against human α-enolase and streptococcal α-enolase. Immunoblot analysis and matrix-assisted laser desorption ionisation-time-of-flight mass spectrometry were used to identify and recombine other streptococcal antigens. Results. Specific positive signals against recombinant human α-enolase were detected by IgM ELISA of serum samples from 50% of BD, 14.3% of SLE, 57.1% of DM, 42.9% of RA, and 57.1% of TA patients. Specific positive signals against streptococcal α-enolase were detected from 42.9% of BD, 14.3% of DM, and 14.3% of TA patients. No SLE and RA sera reacted against streptococcal a-enolase antigen. Streptococcal proteins reacting with sera were identified as hypothetical protein (HP) for SLE and DM patients, acid phosphatase (AP) for RA patients, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) for TA patients. Conclusions. We observed that RA patients did not present serum reactivity against either HP or GAPDH though BD, SLE, DM, and TA patients did. Also, AP reacted with sera from BD, SLE, DM, RA, and TA patients.

AB - Objective. We evaluated the reactivity of sera from Behçet's disease (BD), systemic lupus erythematosus (SLE), dermatomyositis (DM), rheumatoid arthritis (RA), and Takayasu's arteritis (TA) patients against human α-enolase and streptococcal α-enolase, and identified additional streptococcal antigens. Methods. Enzyme-linked immunosorbent assay (ELISA) and immunoblotting were performed using sera from patients with BD, SLE, DM, RA, and TA and healthy volunteers (control) against human α-enolase and streptococcal α-enolase. Immunoblot analysis and matrix-assisted laser desorption ionisation-time-of-flight mass spectrometry were used to identify and recombine other streptococcal antigens. Results. Specific positive signals against recombinant human α-enolase were detected by IgM ELISA of serum samples from 50% of BD, 14.3% of SLE, 57.1% of DM, 42.9% of RA, and 57.1% of TA patients. Specific positive signals against streptococcal α-enolase were detected from 42.9% of BD, 14.3% of DM, and 14.3% of TA patients. No SLE and RA sera reacted against streptococcal a-enolase antigen. Streptococcal proteins reacting with sera were identified as hypothetical protein (HP) for SLE and DM patients, acid phosphatase (AP) for RA patients, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) for TA patients. Conclusions. We observed that RA patients did not present serum reactivity against either HP or GAPDH though BD, SLE, DM, and TA patients did. Also, AP reacted with sera from BD, SLE, DM, RA, and TA patients.

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