Cell-surface Interactions of Echovirus 22

Echovirus 22 (EV22) is a picornavirus forming a distinct molecular cluster together with echovirus 23. EV22 has an Arg-Gly-Asp (RGD) peptide motif in its capsid protein VP1; similar motifs are known to mediate many cell-cell and microbe-host interactions. To identify peptide sequences that specifica...

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Bibliographic Details
Published in:The Journal of biological chemistry 1997-08, Vol.272 (34), p.21176-21180
Main Authors: Pulli, Timo, Koivunen, Erkki, Hyypiä, Timo
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Capsid - chemistry
Collagenases - physiology
Consensus Sequence
Enterovirus - chemistry
Enterovirus - growth & development
Enterovirus B, Human - chemistry
Enterovirus B, Human - growth & development
Humans
Immunologic Techniques
Integrins - physiology
Matrix Metalloproteinase 9
Molecular Sequence Data
Oligopeptides
Peptide Library
Receptors, Virus - metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Tumor Cells, Cultured
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Summary:Echovirus 22 (EV22) is a picornavirus forming a distinct molecular cluster together with echovirus 23. EV22 has an Arg-Gly-Asp (RGD) peptide motif in its capsid protein VP1; similar motifs are known to mediate many cell-cell and microbe-host interactions. To identify peptide sequences that specifically bind to EV22 and potentially play a role in receptor recognition, we have used here peptide libraries displayed in filamentous phage. We isolated an EV22-binding motif CLRSG(R/F)GC. The synthetic CLRSGRGC peptide was able to inhibit EV22 infection. The infection was also inhibited by an RGD-containing peptide representing the C terminus of the EV22 capsid protein VP1 and CWDDGWLC (an RGD-binding peptide; Pasqualini, R., Koivunen, E., and Ruoslahti, E. (1995) J. Cell Biol. 130, 1189–1196). As the EV22-recognizing sequence LRSG is found in the integrin β1 chain and the entire LRSGRG hexapeptide occurs in the matrix metalloproteinase 9 (MMP-9), we carried out blocking experiments with anti-integrin and anti-MMP-9 antibodies. EV22 infection could be blocked in cell cultures with anti-αv, -β1, and, to a lesser extent, with anti-MMP-9 antibodies. These results imply that EV22 recognizes preferentially αvβ1-integrin as a cellular receptor and MMP-9 may also play a role in the cell-surface interactions of the virus.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.272.34.21176