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Peptide mimicrying between SARS coronavirus spike protein and human proteins reacts with SARS patient serum.

Hwa KY, Lin WM, Hou YI, Yeh TM - J. Biomed. Biotechnol. (2008)

Bottom Line: The spike (S) protein of SARS-CoV plays an important role in the virus entry into a cell.In this study, eleven synthetic peptides from the S protein were selected based on its sequence homology with human proteins.Another peptide D10 (residues 490-502) stimulated A549 to proliferate and secrete IL-8.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Science and Engineering, Center for Biomedical Industries, National Taipei University of Technology, Taipei 106, Taiwan.

ABSTRACT
Molecular mimicry, defined as similar structures shared by molecules from dissimilar genes or proteins, is a general strategy used by pathogens to infect host cells. Severe acute respiratory syndrome (SARS) is a new human respiratory infectious disease caused by SARS coronavirus (SARS-CoV). The spike (S) protein of SARS-CoV plays an important role in the virus entry into a cell. In this study, eleven synthetic peptides from the S protein were selected based on its sequence homology with human proteins. Two of the peptides D07 (residues 927-937) and D08 (residues 942-951) were recognized by the sera of SARS patients. Murine hyperimmune sera against these peptides bound to proteins of human lung epithelial cells A549. Another peptide D10 (residues 490-502) stimulated A549 to proliferate and secrete IL-8. The present results suggest that the selected S protein regions, which share sequence homology with human proteins, may play important roles in SARS-CoV infection.

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Related in: MedlinePlus

Antibody binding activity of SARS patients' sera todifferent peptides. Sera of SARS patients at convalescent stage as well asnormal controls were collected as described in Section 2. Antibodies binding to different peptides were detected by ELISA as described in Section 2. BK represents bradykinin. “∗” indicates P < .05.
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fig3: Antibody binding activity of SARS patients' sera todifferent peptides. Sera of SARS patients at convalescent stage as well asnormal controls were collected as described in Section 2. Antibodies binding to different peptides were detected by ELISA as described in Section 2. BK represents bradykinin. “∗” indicates P < .05.

Mentions: Eleven peptides (D01–D11, see Table 1), which represent those pathogenic regions weresynthesized as well as bradykinin and Ang I were tested to see whether those peptidescan be recognized by SARS patients' sera.The peptides were designed based on the algorithms predicting immunogenicity,second structure, protein topology, and hydrophobicity. Our goal is to select for peptides with highimmunogenicity, with location on the protein surface, and with low hydrophobicity. The designed peptide sequences weresynthesized and tested with clinical samples of SARS patient sera. A significant increase of SARS patients' serabinding to peptide D01, D07, and D08 was found as compared to the binding ofnormal sera (see Figure 3).


Peptide mimicrying between SARS coronavirus spike protein and human proteins reacts with SARS patient serum.

Hwa KY, Lin WM, Hou YI, Yeh TM - J. Biomed. Biotechnol. (2008)

Antibody binding activity of SARS patients' sera todifferent peptides. Sera of SARS patients at convalescent stage as well asnormal controls were collected as described in Section 2. Antibodies binding to different peptides were detected by ELISA as described in Section 2. BK represents bradykinin. “∗” indicates P < .05.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2254527&req=5

fig3: Antibody binding activity of SARS patients' sera todifferent peptides. Sera of SARS patients at convalescent stage as well asnormal controls were collected as described in Section 2. Antibodies binding to different peptides were detected by ELISA as described in Section 2. BK represents bradykinin. “∗” indicates P < .05.
Mentions: Eleven peptides (D01–D11, see Table 1), which represent those pathogenic regions weresynthesized as well as bradykinin and Ang I were tested to see whether those peptidescan be recognized by SARS patients' sera.The peptides were designed based on the algorithms predicting immunogenicity,second structure, protein topology, and hydrophobicity. Our goal is to select for peptides with highimmunogenicity, with location on the protein surface, and with low hydrophobicity. The designed peptide sequences weresynthesized and tested with clinical samples of SARS patient sera. A significant increase of SARS patients' serabinding to peptide D01, D07, and D08 was found as compared to the binding ofnormal sera (see Figure 3).

Bottom Line: The spike (S) protein of SARS-CoV plays an important role in the virus entry into a cell.In this study, eleven synthetic peptides from the S protein were selected based on its sequence homology with human proteins.Another peptide D10 (residues 490-502) stimulated A549 to proliferate and secrete IL-8.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Science and Engineering, Center for Biomedical Industries, National Taipei University of Technology, Taipei 106, Taiwan.

ABSTRACT
Molecular mimicry, defined as similar structures shared by molecules from dissimilar genes or proteins, is a general strategy used by pathogens to infect host cells. Severe acute respiratory syndrome (SARS) is a new human respiratory infectious disease caused by SARS coronavirus (SARS-CoV). The spike (S) protein of SARS-CoV plays an important role in the virus entry into a cell. In this study, eleven synthetic peptides from the S protein were selected based on its sequence homology with human proteins. Two of the peptides D07 (residues 927-937) and D08 (residues 942-951) were recognized by the sera of SARS patients. Murine hyperimmune sera against these peptides bound to proteins of human lung epithelial cells A549. Another peptide D10 (residues 490-502) stimulated A549 to proliferate and secrete IL-8. The present results suggest that the selected S protein regions, which share sequence homology with human proteins, may play important roles in SARS-CoV infection.

Show MeSH
Related in: MedlinePlus