Journal
VIRUS RESEARCH
Volume 147, Issue 2, Pages 294-299Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.virusres.2009.11.016
Keywords
PRRS; E protein; Infectious clone; Myristoylation; Fatty acid acylation
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Funding
- National Research Initiatives of the US Department of Agriculture Cooperative State Research Education and Extension Service [2008-35204-04634]
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The small envelope (E) protein of porcine reproductive and respiratory syndrome virus (PRRSV) is known to possess the properties of an ion-channel protein, and in the present study we show that the PRRSV E protein is N-terminal myristoylated. The PRRSV E protein contains the consensus motif of (1)MGXXXS(6) for myristoylation, and in the presence of 2-hydroxymyristic acid, the virus titer decreased by 2.5 log TCID50 and the level of viral RNA was reduced significantly. When the glycine at position 2 was mutated to alanine (G2A) using an infectious cDNA clone, a viable virus was recoverable and a mutant PRRSV was obtained. The titers of G2A mutant virus were 2.0 x 10(4) and 1.0 x 10(6) TCID50/ml for 'passage-2' and 'passage-3' viruses, respectively, in PAM cells, and these titers were significantly lower than those of wild-type PRRSV. When treated with the myristoylation inhibitor, the G2A mutant virus was resistant to the drug. The data show that the PRRSV E protein myristoylation is non-essential for PRRSV infectivity but promotes the growth of the virus. (C) 2009 Elsevier B.V. All rights reserved.
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