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Related Experiment Videos

Cell-surface interactions of echovirus 22

T Pulli1, E Koivunen, T Hyypiä

  • 1National Public Health Institute, Mannerheimintie 166, FIN-00300 Helsinki, Finland. timo.pulli@ktl.fi

The Journal of Biological Chemistry
|August 22, 1997
PubMed
Summary

Echovirus 22 (EV22) uses the alphavbeta1-integrin as its primary cellular receptor, with matrix metalloproteinase-9 (MMP-9) also potentially involved in its cell surface interactions. This finding aids in understanding viral entry mechanisms.

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Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Echovirus 22 (EV22), a picornavirus, possesses an Arg-Gly-Asp (RGD) motif in its VP1 capsid protein, crucial for host-cell interactions.
  • RGD motifs are known to mediate diverse cell-cell and microbe-host interactions, suggesting a role in EV22's receptor recognition.

Purpose of the Study:

  • To identify specific peptide sequences that bind to EV22.
  • To elucidate the role of these peptides in viral receptor recognition and infection mechanisms.

Main Methods:

  • Phage display peptide libraries were employed to isolate EV22-binding motifs.
  • Synthetic peptides and blocking antibodies against integrins and MMP-9 were used to inhibit EV22 infection.

Main Results:

  • A novel EV22-binding motif, CLRSG(R/F)GC, was isolated, with the synthetic peptide CLRSGRGC inhibiting EV22 infection.
  • Infection was also inhibited by an RGD-containing peptide from EV22 VP1 and a known RGD-binding peptide.
  • Blocking experiments demonstrated that anti-alphav, anti-beta1, and anti-MMP-9 antibodies could inhibit EV22 infection.

Conclusions:

  • EV22 preferentially recognizes alphavbeta1-integrin as its cellular receptor.
  • Matrix metalloproteinase-9 (MMP-9) may also contribute to EV22's cell-surface interactions and subsequent infection.

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