Proteomic analysis of endothelial cell autoantigens recognized by anti-dengue virus nonstructural protein 1 antibodies

Hsien Jen Cheng, Chiou Feng Lin, Huan Yao Lei, Hsiao Sheng Liu, Trai Ming Yeh, Yueh Hsia Luo, Yee Shin Lin

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

We previously showed the occurrence of autoimmune responses in dengue virus (DV) infection, which has potential implications for the pathogenesis of dengue hemorrhagic syndrome. In the present study, we have used a proteomic analysis to identify several candidate proteins on HMEC-1 endothelial cells recognized by anti-DV nonstructural protein 1 (NS1) antibodies. The target proteins, including ATP synthase β chain, protein disulfide isomerase, vimentin, and heat shock protein 60, co-localize with anti-NS1 binding sites on nonfixed HMEC-1 cells using immunohistochemical double staining and confocal microscopy. The cross-reactivity of anti-target protein antibodies with HMEC-1 cells was inhibited by NS1 protein preabsorption. Furthermore, a cross-reactive epitope on NS1 amino acid residues 311-330 (P311-330) was predicted using homologous sequence alignment. The reactivity of dengue hemorrhagic patient sera with HMEC-1 cells was blocked by synthetic peptide P311-330 pre-absorption. Taken together, our results identify putative targets on endothelial cells recognized by anti-DV NS1 antibodies, where NS1 P311-330 possesses the shared epitope.

Original languageEnglish
Pages (from-to)63-73
Number of pages11
JournalExperimental Biology and Medicine
Volume234
Issue number1
DOIs
Publication statusPublished - Jan 2009
Externally publishedYes

Fingerprint

Dengue Virus
Endothelial cells
Autoantigens
Viruses
Proteomics
Endothelial Cells
Antibodies
Proteins
Severe Dengue
Epitopes
Chaperonin 60
Protein Disulfide-Isomerases
Sequence Alignment
Vimentin
Virus Diseases
Sequence Homology
Confocal microscopy
Autoimmunity
Protein Binding
Confocal Microscopy

Keywords

  • Autoantibodies
  • Dengue virus
  • Endothelial cell autoantigens
  • Proteomic analysis

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Proteomic analysis of endothelial cell autoantigens recognized by anti-dengue virus nonstructural protein 1 antibodies. / Cheng, Hsien Jen; Lin, Chiou Feng; Lei, Huan Yao; Liu, Hsiao Sheng; Yeh, Trai Ming; Luo, Yueh Hsia; Lin, Yee Shin.

In: Experimental Biology and Medicine, Vol. 234, No. 1, 01.2009, p. 63-73.

Research output: Contribution to journalArticle

Cheng, Hsien Jen ; Lin, Chiou Feng ; Lei, Huan Yao ; Liu, Hsiao Sheng ; Yeh, Trai Ming ; Luo, Yueh Hsia ; Lin, Yee Shin. / Proteomic analysis of endothelial cell autoantigens recognized by anti-dengue virus nonstructural protein 1 antibodies. In: Experimental Biology and Medicine. 2009 ; Vol. 234, No. 1. pp. 63-73.
@article{69dc164abd3b42329d4f8ffe6b095e77,
title = "Proteomic analysis of endothelial cell autoantigens recognized by anti-dengue virus nonstructural protein 1 antibodies",
abstract = "We previously showed the occurrence of autoimmune responses in dengue virus (DV) infection, which has potential implications for the pathogenesis of dengue hemorrhagic syndrome. In the present study, we have used a proteomic analysis to identify several candidate proteins on HMEC-1 endothelial cells recognized by anti-DV nonstructural protein 1 (NS1) antibodies. The target proteins, including ATP synthase β chain, protein disulfide isomerase, vimentin, and heat shock protein 60, co-localize with anti-NS1 binding sites on nonfixed HMEC-1 cells using immunohistochemical double staining and confocal microscopy. The cross-reactivity of anti-target protein antibodies with HMEC-1 cells was inhibited by NS1 protein preabsorption. Furthermore, a cross-reactive epitope on NS1 amino acid residues 311-330 (P311-330) was predicted using homologous sequence alignment. The reactivity of dengue hemorrhagic patient sera with HMEC-1 cells was blocked by synthetic peptide P311-330 pre-absorption. Taken together, our results identify putative targets on endothelial cells recognized by anti-DV NS1 antibodies, where NS1 P311-330 possesses the shared epitope.",
keywords = "Autoantibodies, Dengue virus, Endothelial cell autoantigens, Proteomic analysis",
author = "Cheng, {Hsien Jen} and Lin, {Chiou Feng} and Lei, {Huan Yao} and Liu, {Hsiao Sheng} and Yeh, {Trai Ming} and Luo, {Yueh Hsia} and Lin, {Yee Shin}",
year = "2009",
month = "1",
doi = "10.3181/0805-RM-147",
language = "English",
volume = "234",
pages = "63--73",
journal = "Experimental Biology and Medicine",
issn = "1535-3702",
publisher = "SAGE Publications Ltd",
number = "1",

}

TY - JOUR

T1 - Proteomic analysis of endothelial cell autoantigens recognized by anti-dengue virus nonstructural protein 1 antibodies

AU - Cheng, Hsien Jen

AU - Lin, Chiou Feng

AU - Lei, Huan Yao

AU - Liu, Hsiao Sheng

AU - Yeh, Trai Ming

AU - Luo, Yueh Hsia

AU - Lin, Yee Shin

PY - 2009/1

Y1 - 2009/1

N2 - We previously showed the occurrence of autoimmune responses in dengue virus (DV) infection, which has potential implications for the pathogenesis of dengue hemorrhagic syndrome. In the present study, we have used a proteomic analysis to identify several candidate proteins on HMEC-1 endothelial cells recognized by anti-DV nonstructural protein 1 (NS1) antibodies. The target proteins, including ATP synthase β chain, protein disulfide isomerase, vimentin, and heat shock protein 60, co-localize with anti-NS1 binding sites on nonfixed HMEC-1 cells using immunohistochemical double staining and confocal microscopy. The cross-reactivity of anti-target protein antibodies with HMEC-1 cells was inhibited by NS1 protein preabsorption. Furthermore, a cross-reactive epitope on NS1 amino acid residues 311-330 (P311-330) was predicted using homologous sequence alignment. The reactivity of dengue hemorrhagic patient sera with HMEC-1 cells was blocked by synthetic peptide P311-330 pre-absorption. Taken together, our results identify putative targets on endothelial cells recognized by anti-DV NS1 antibodies, where NS1 P311-330 possesses the shared epitope.

AB - We previously showed the occurrence of autoimmune responses in dengue virus (DV) infection, which has potential implications for the pathogenesis of dengue hemorrhagic syndrome. In the present study, we have used a proteomic analysis to identify several candidate proteins on HMEC-1 endothelial cells recognized by anti-DV nonstructural protein 1 (NS1) antibodies. The target proteins, including ATP synthase β chain, protein disulfide isomerase, vimentin, and heat shock protein 60, co-localize with anti-NS1 binding sites on nonfixed HMEC-1 cells using immunohistochemical double staining and confocal microscopy. The cross-reactivity of anti-target protein antibodies with HMEC-1 cells was inhibited by NS1 protein preabsorption. Furthermore, a cross-reactive epitope on NS1 amino acid residues 311-330 (P311-330) was predicted using homologous sequence alignment. The reactivity of dengue hemorrhagic patient sera with HMEC-1 cells was blocked by synthetic peptide P311-330 pre-absorption. Taken together, our results identify putative targets on endothelial cells recognized by anti-DV NS1 antibodies, where NS1 P311-330 possesses the shared epitope.

KW - Autoantibodies

KW - Dengue virus

KW - Endothelial cell autoantigens

KW - Proteomic analysis

UR - http://www.scopus.com/inward/record.url?scp=60549094971&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=60549094971&partnerID=8YFLogxK

U2 - 10.3181/0805-RM-147

DO - 10.3181/0805-RM-147

M3 - Article

C2 - 18997103

AN - SCOPUS:60549094971

VL - 234

SP - 63

EP - 73

JO - Experimental Biology and Medicine

JF - Experimental Biology and Medicine

SN - 1535-3702

IS - 1

ER -