Temporal correlation between a single amino acid change in the VP4 of a porcine rotavirus and a marked change in pathogenicity

B Burke, J C Bridger, U Desselberger

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

We previously described a marked increase in the pathogenicity of a cell culture grown porcine rotavirus, PRV 4F, during serial passage in gnotobiotic piglets (Bridger et al., 1992). Here we report close temporal correlation between this change in pathogenicity and an amino acid change within a highly conserved hydrophobic domain of VP4 at position 469. Cell culture grown PRV 4F is unique in having a hydrophilic residue, glutamine, at amino acid 469; all previously sequenced VP4s have hydrophobic leucine or phenylalanine residues at the corresponding position. The detection of a point mutation causing a deduced amino acid change from glutamine to leucine at amino acid 469 of PRV 4F VP4 in virus obtained from one piglet at the second serial passage correlated exactly with the emergence of viral pathogenicity. However, given the multifactorial nature of virus pathogenicity, genetic studies are required to ascertain the degree to which this mutation is responsible for the observed change in pathogenicity.

Original languageEnglish
Pages (from-to)754-759
Number of pages6
JournalVirology
Volume202
Issue number2
DOIs
Publication statusPublished - 1 Aug 1994
Externally publishedYes

Fingerprint

Rotavirus
Virulence
Swine
Amino Acids
Serial Passage
Glutamine
Leucine
Cell Culture Techniques
Germ-Free Life
Viruses
Phenylalanine
Point Mutation
Mutation

Keywords

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Capsid/genetics
  • Capsid Proteins
  • DNA Primers/chemistry
  • Molecular Sequence Data
  • Mutation
  • Rotavirus/pathogenicity
  • Rotavirus Infections/veterinary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Solubility
  • Swine
  • Swine Diseases/microbiology

Cite this

Temporal correlation between a single amino acid change in the VP4 of a porcine rotavirus and a marked change in pathogenicity. / Burke, B; Bridger, J C; Desselberger, U.

In: Virology, Vol. 202, No. 2, 01.08.1994, p. 754-759.

Research output: Contribution to journalArticle

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abstract = "We previously described a marked increase in the pathogenicity of a cell culture grown porcine rotavirus, PRV 4F, during serial passage in gnotobiotic piglets (Bridger et al., 1992). Here we report close temporal correlation between this change in pathogenicity and an amino acid change within a highly conserved hydrophobic domain of VP4 at position 469. Cell culture grown PRV 4F is unique in having a hydrophilic residue, glutamine, at amino acid 469; all previously sequenced VP4s have hydrophobic leucine or phenylalanine residues at the corresponding position. The detection of a point mutation causing a deduced amino acid change from glutamine to leucine at amino acid 469 of PRV 4F VP4 in virus obtained from one piglet at the second serial passage correlated exactly with the emergence of viral pathogenicity. However, given the multifactorial nature of virus pathogenicity, genetic studies are required to ascertain the degree to which this mutation is responsible for the observed change in pathogenicity.",
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N2 - We previously described a marked increase in the pathogenicity of a cell culture grown porcine rotavirus, PRV 4F, during serial passage in gnotobiotic piglets (Bridger et al., 1992). Here we report close temporal correlation between this change in pathogenicity and an amino acid change within a highly conserved hydrophobic domain of VP4 at position 469. Cell culture grown PRV 4F is unique in having a hydrophilic residue, glutamine, at amino acid 469; all previously sequenced VP4s have hydrophobic leucine or phenylalanine residues at the corresponding position. The detection of a point mutation causing a deduced amino acid change from glutamine to leucine at amino acid 469 of PRV 4F VP4 in virus obtained from one piglet at the second serial passage correlated exactly with the emergence of viral pathogenicity. However, given the multifactorial nature of virus pathogenicity, genetic studies are required to ascertain the degree to which this mutation is responsible for the observed change in pathogenicity.

AB - We previously described a marked increase in the pathogenicity of a cell culture grown porcine rotavirus, PRV 4F, during serial passage in gnotobiotic piglets (Bridger et al., 1992). Here we report close temporal correlation between this change in pathogenicity and an amino acid change within a highly conserved hydrophobic domain of VP4 at position 469. Cell culture grown PRV 4F is unique in having a hydrophilic residue, glutamine, at amino acid 469; all previously sequenced VP4s have hydrophobic leucine or phenylalanine residues at the corresponding position. The detection of a point mutation causing a deduced amino acid change from glutamine to leucine at amino acid 469 of PRV 4F VP4 in virus obtained from one piglet at the second serial passage correlated exactly with the emergence of viral pathogenicity. However, given the multifactorial nature of virus pathogenicity, genetic studies are required to ascertain the degree to which this mutation is responsible for the observed change in pathogenicity.

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KW - Mutation

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KW - Rotavirus Infections/veterinary

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