Substitution of leucine 8 in the simian immunodeficiency virus matrix protein impairs particle formation without affecting N-myristylation of the Gag precursor

Virology
S A González, J L Affranchino

Abstract

In the late stages of replication of the simian immunodeficiency viruses (SIV), the matrix protein (MA) plays a central role in the transport of Pr55gag to the plasma membrane, assembly of virus particles, and incorporation of the envelope glycoprotein into particles. Targeting of Pr55gag to the plasma membrane is mediated by two motifs within the MA protein: the N-terminal myristate and a cluster of positively charged amino acids. In this report, we characterized the assembly phenotype of an SIV Gag mutant (L8Q) carrying the single amino acid substitution of glutamine for leucine at position 8 in the MA domain. The hydropathic profile of the mutated MA protein indicated that the L8Q amino acid change disrupts the hydrophobic character of the region comprising the first 10 residues of the protein. Expression of mutant L8Q Gag protein in CV-1 cells, by means of the vaccinia virus vector system, resulted in efficient synthesis and N-myristylation of Pr55gag. However, this mutation severely impaired particle production, as inferred from both biochemical and electron microscopy analyses. Cellular fractionation assays revealed that in cells expressing mutant L8Q, the proportion of cytosol-associated Pr55gag was significantly increas...Continue Reading

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Citations

Oct 26, 2010·AIDS Research and Human Retroviruses·María L RauddiSilvia A González
Jul 23, 2002·Journal of Virology·Huating WangLouis M Mansky
Dec 14, 2011·Viruses·Julia C Kenyon, Andrew M L Lever
May 30, 2001·Virus Research·M L ManriqueJ L Affranchino
Jun 26, 2007·Advances in Pharmacology·Catherine S Adamson, Eric O Freed
May 24, 2014·The Journal of General Virology·Juan C Abdusetir CerfoglioJosé L Affranchino
Jan 31, 2002·AIDS·H G Göttlinger

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