A second RGD motif in the 1D capsid protein of a SAT1 type foot-and-mouth disease virus field isolate is not

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P Storey1, J Theron, F F Maree

  • 1Onderstepoort Veterinary Institute, Exotic Diseases Division, Private Bag X05, Onderstepoort 0010, South Africa.

Virus Research
|December 13, 2006
PubMed

Insights

The foot-and-mouth disease virus (FMDV) 1D protein has two Arg-Gly-Asp (RGD) motifs. Only the betaG-betaH loop RGD is essential for FMDV binding and infection of susceptible cells.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • The Arg-Gly-Asp (RGD) motif in the foot-and-mouth disease virus (FMDV) 1D protein is crucial for cell binding.
  • A FMDV SAT1 isolate (NAM/307/98) possesses a second, upstream RGD motif in its 1D protein.

Purpose of the Study:

  • To investigate the functional role of the two RGD motifs in FMDV infection.
  • To determine if the second RGD motif contributes to FMDV cell binding and infectivity.

Main Methods:

  • Site-directed mutagenesis of the FMDV 1D protein's RGD motifs using infectious chimeric cDNA clones.
  • Assessing viral infectivity in baby hamster kidney (BHK-21) cells.
  • Confirming viral RNA replication and particle production via molecular and electron microscopy techniques.

Main Results:

  • Mutating the betaG-betaH loop RGD to KGE abolished viral infectivity in BHK-21 cells.
  • Restoring the RGD sequence in the betaG-betaH loop rescued viral infectivity.
  • Viral RNA replication and particle formation were observed in both mutant and non-mutant viruses, indicating the second RGD motif is not essential for these processes.

Conclusions:

  • The conserved betaG-betaH loop RGD motif is essential for FMDV binding to susceptible cells.
  • The second RGD motif identified in the FMDV 1D protein of isolate NAM/307/98 does not play a significant role in receptor binding or infectivity in BHK-21 cells.

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