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Facilitation of cell adhesion by immobilized dengue viral nonstructural protein 1 (NS1): arginine-glycine-aspartic acid structural mimicry within the dengue viral NS1 antigen.
J Infect Dis. 2002 Sep 15; 186(6):743-51.JI

Abstract

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.

Authors+Show Affiliations

Institute of Molecular and Cellular Biology, Tzu-Chi University, Hualien, and Institute of Preventive Medicine, National Defense Medical Center, Taipei, Taiwan, Republic of China. hhchang@mail.tcu.edu.twNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12198607

Citation

Chang, Hsin-Hou, et al. "Facilitation of Cell Adhesion By Immobilized Dengue Viral Nonstructural Protein 1 (NS1): Arginine-glycine-aspartic Acid Structural Mimicry Within the Dengue Viral NS1 Antigen." The Journal of Infectious Diseases, vol. 186, no. 6, 2002, pp. 743-51.
Chang HH, Shyu HF, Wang YM, et al. Facilitation of cell adhesion by immobilized dengue viral nonstructural protein 1 (NS1): arginine-glycine-aspartic acid structural mimicry within the dengue viral NS1 antigen. J Infect Dis. 2002;186(6):743-51.
Chang, H. H., Shyu, H. F., Wang, Y. M., Sun, D. S., Shyu, R. H., Tang, S. S., & Huang, Y. S. (2002). Facilitation of cell adhesion by immobilized dengue viral nonstructural protein 1 (NS1): arginine-glycine-aspartic acid structural mimicry within the dengue viral NS1 antigen. The Journal of Infectious Diseases, 186(6), 743-51.
Chang HH, et al. Facilitation of Cell Adhesion By Immobilized Dengue Viral Nonstructural Protein 1 (NS1): Arginine-glycine-aspartic Acid Structural Mimicry Within the Dengue Viral NS1 Antigen. J Infect Dis. 2002 Sep 15;186(6):743-51. PubMed PMID: 12198607.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Facilitation of cell adhesion by immobilized dengue viral nonstructural protein 1 (NS1): arginine-glycine-aspartic acid structural mimicry within the dengue viral NS1 antigen. AU - Chang,Hsin-Hou, AU - Shyu,Huey-Fen, AU - Wang,Yo-Ming, AU - Sun,Der-Shan, AU - Shyu,Rong-Hwa, AU - Tang,Shiao-Shek, AU - Huang,Yao-Shine, Y1 - 2002/08/28/ PY - 2002/02/04/received PY - 2002/05/09/revised PY - 2002/8/29/pubmed PY - 2002/10/17/medline PY - 2002/8/29/entrez SP - 743 EP - 51 JF - The Journal of infectious diseases JO - J Infect Dis VL - 186 IS - 6 N2 - 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. SN - 0022-1899 UR - https://www.unboundmedicine.com/medline/citation/12198607/Facilitation_of_cell_adhesion_by_immobilized_dengue_viral_nonstructural_protein_1__NS1_:_arginine_glycine_aspartic_acid_structural_mimicry_within_the_dengue_viral_NS1_antigen_ L2 - https://academic.oup.com/jid/article-lookup/doi/10.1086/342600 DB - PRIME DP - Unbound Medicine ER -