Facilitation of cell adhesion by immobilized dengue viral nonstructural protein 1 (NS1): Arginine-glycine-aspartic acid structural mimicry within the dengue viral NS1 antigen

被引：54

作者：

Chang, HH ^{[1
]}

Shyu, HF

Wang, YM

Sun, DS

Shyu, RH

Tang, SS

Huang, YS

机构：

[1] Tzu Chi Univ, Inst Mol & Cellular Biol, Hualien 970, Taiwan

[2] Tzu Chi Univ, Inst Human Genet, Hualien 970, Taiwan

[3] Natl Def Med Ctr, Inst Prevent Med, Taipei, Taiwan

来源：

JOURNAL OF INFECTIOUS DISEASES | 2002年 / 186卷 / 06期

关键词：

D O I：

10.1086/342600

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Dengue virus infection causes life-threatening hemorrhagic fever. Increasing evidence implies that dengue viral nonstructural protein 1 (NS1) exhibits a tendency to elicit potentially hazardous autoantibodies, which show a wide spectrum of specificity against extracellular matrix and platelet antigens. How NS1 elicits autoantibodies remains unclear. To address the hypothesis that NS1 and matrix proteins may have structural and functional similarity, cell-matrix and cell-NS1 interactions were evaluated using a cell-adhesion assay. The present study showed that dengue NS1 immobilized on coverslips resulted in more cell adhesion than did the control proteins. This cell adhesion was inhibited by peptides containing arginine-glycine-aspartic acid (RGD), a motif important for integrin-mediated cell adhesion. In addition, anti-NS1 antibodies blocked RGD-mediated cell adhesion. Although there is no RGD motif in the NS1 protein sequence, these data indicate that RGD structural mimicry exists within the NS1 antigen.

引用

页码：743 / 751

页数：9

共 55 条

[1] CELLULAR-IMMUNITY TO A DETERMINANT COMMON TO GLUTAMATE-DECARBOXYLASE AND COXSACKIE-VIRUS IN INSULIN-DEPENDENT DIABETES [J].

ATKINSON, MA ;

BOWMAN, MA ;

CAMPBELL, L ;

DARROW, BL ;

KAUFMAN, DL ;

MACLAREN, NK .

JOURNAL OF CLINICAL INVESTIGATION, 1994, 94 (05) :2125-2129

[2]

Avirutnan P, 1998, J IMMUNOL, V161, P6338

[3] Molecular mimicry in the MHC. Hidden clues to autoimmunity? [J].

Baum, H ;

Davies, H ;

Peakman, M .

IMMUNOLOGY TODAY, 1996, 17 (02) :64-70

[4] CELL-SURFACE RECEPTORS FOR EXTRACELLULAR-MATRIX MOLECULES [J].

BUCK, CA ;

HORWITZ, AF .

ANNUAL REVIEW OF CELL BIOLOGY, 1987, 3 :179-205

[5] Positional importance of Pro53 adjacent to the Arg49-Gly50-Asp51 sequence of rhodostomin in binding to integrin αIIbβ3 [J].

Chang, CP ;

Chang, JC ;

Chang, HH ;

Tsai, WJ ;

Lo, SCJ .

BIOCHEMICAL JOURNAL, 2001, 357 :57-64

[6] RHODOSTOMIN, AN RGD-CONTAINING PEPTIDE EXPRESSED FROM A SYNTHETIC GENE IN ESCHERICHIA-COLI, FACILITATES THE ATTACHMENT OF HUMAN HEPATOMA-CELLS [J].

CHANG, HH ;

HU, ST ;

HUANG, TF ;

CHEN, SH ;

LEE, YHW ;

LO, SCJ .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1993, 190 (01) :242-249

[7] Application of recombinant rhodostomin in studying cell adhesion [J].

Chang, HH ;

Chang, CP ;

Chang, JC ;

Dung, SZ ;

Lo, SJ .

JOURNAL OF BIOMEDICAL SCIENCE, 1997, 4 (05) :235-243

[8] Recombinant rhodostomin substrates induce transformation and active calcium oscillation in human platelets [J].

Chang, HH ;

Lin, CH ;

Lo, SJ .

EXPERIMENTAL CELL RESEARCH, 1999, 250 (02) :387-400

[9] Glutathione S-transferase-rhodostomin fusion protein inhibits platelet aggregation and induces platelet shape change [J].

Chang, HH ;

Tsai, WJ ;

Lo, SCJ .

TOXICON, 1997, 35 (02) :195-204

[10] Full-spreading platelets induced by the recombinant rhodostomin are via binding to integrins and correlated with FAK phosphorylation [J].

Chang, HH ;

Lo, SJ .

TOXICON, 1998, 36 (08) :1087-1099

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