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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

mprF  -  hypothetical protein

Staphylococcus aureus RF122

 
 
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Disease relevance of mprF

  • Another VirR-regulated gene is homologous to mprF, which encodes a protein that modifies membrane phosphatidyl glycerol with l-lysine and that is involved in resistance to human defensins in Staphylococcus aureus [1].
  • We demonstrate here that expression of mprF is sufficient to confer L-PG production in Escherichia coli, which indicates that MprF represents the L-PG synthase [2].
 

High impact information on mprF

  • An mprF mutant strain was killed considerably faster by human neutrophils and exhibited attenuated virulence in mice, indicating a key role for defensin resistance in the pathogenicity of S. aureus [3].
  • In addition, the mprF mutant exhibited an increased amount of origin per cell in vivo, suggesting that LPG is involved in regulating the cell cycle event(s) [4].
  • To further delineate charge properties of the bacterial envelope important in Group IIA PLA(2) action against S. aureus, we examined the effects of mutations that prevent specific modifications of cell wall (dltA) and cell membrane (mprF) polyanions [5].
  • This study examined whether the Staphylococcus aureus mprF gene encodes LPG synthetase [6].
  • Expression of tcaA and mprF and glycopeptide resistance in clinical glycopeptide-intermediate Staphylococcus aureus (GISA) and heteroGISA strains [7].
 

Biological context of mprF

 

Anatomical context of mprF

  • The inactivation of mprF by Tn917 insertion in HT2002 0127 caused a significant increase in the binding of vancomycin to the cell membranes [8].
 

Associations of mprF with chemical compounds

  • A crude membrane fraction prepared from wild-type S. aureus cells had LPG synthetase activity that depended on PG and lysyl-tRNA, whereas the membrane fraction from an mprF deletion mutant did not [6].
 

Analytical, diagnostic and therapeutic context of mprF

  • Northern blot analysis, insertional inactivation and complementation experiments showed that mprF mediates vancomycin susceptibility in S. aureus [8].

References

  1. VirR, a response regulator critical for Listeria monocytogenes virulence. Mandin, P., Fsihi, H., Dussurget, O., Vergassola, M., Milohanic, E., Toledo-Arana, A., Lasa, I., Johansson, J., Cossart, P. Mol. Microbiol. (2005) [Pubmed]
  2. MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance. Staubitz, P., Neumann, H., Schneider, T., Wiedemann, I., Peschel, A. FEMS Microbiol. Lett. (2004) [Pubmed]
  3. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine. Peschel, A., Jack, R.W., Otto, M., Collins, L.V., Staubitz, P., Nicholson, G., Kalbacher, H., Nieuwenhuizen, W.F., Jung, G., Tarkowski, A., van Kessel, K.P., van Strijp, J.A. J. Exp. Med. (2001) [Pubmed]
  4. Inhibitory effects of basic or neutral phospholipid on acidic phospholipid-mediated dissociation of adenine nucleotide bound to DnaA protein, the initiator of chromosomal DNA replication. Ichihashi, N., Kurokawa, K., Matsuo, M., Kaito, C., Sekimizu, K. J. Biol. Chem. (2003) [Pubmed]
  5. Role of charge properties of bacterial envelope in bactericidal action of human group IIA phospholipase A2 against Staphylococcus aureus. Koprivnjak, T., Peschel, A., Gelb, M.H., Liang, N.S., Weiss, J.P. J. Biol. Chem. (2002) [Pubmed]
  6. Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol. Oku, Y., Kurokawa, K., Ichihashi, N., Sekimizu, K. Microbiology (Reading, Engl.) (2004) [Pubmed]
  7. Expression of tcaA and mprF and glycopeptide resistance in clinical glycopeptide-intermediate Staphylococcus aureus (GISA) and heteroGISA strains. Wootton, M., Macgowan, A.P., Walsh, T.R. Biochim. Biophys. Acta (2005) [Pubmed]
  8. Inactivation of mprF affects vancomycin susceptibility in Staphylococcus aureus. Ruzin, A., Severin, A., Moghazeh, S.L., Etienne, J., Bradford, P.A., Projan, S.J., Shlaes, D.M. Biochim. Biophys. Acta (2003) [Pubmed]
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