M Veit


Country: Germany


  1. Veit M, Kabatek A, Tielesch C, Hermann A. Characterization of equine arteritis virus particles and demonstration of their hemolytic activity. Arch Virol. 2008;153:351-6 pubmed publisher
    ..Finally, we provide evidence that EAV possess hemagglutinating and hemolytic activity. The hemolysis assay might be useful for determining which of the surface proteins carries the receptor-binding and membrane fusion activity of EAV. ..
  2. Veit M. Palmitoylation of virus proteins. Biol Cell. 2012;104:493-515 pubmed publisher
    ..The topics are described mainly for palmitoylated proteins of influenza virus, but proteins of other important pathogens, such as the causative agents of AIDS and severe acute respiratory syndrome, and of model viruses are discussed. ..
  3. Veit M, Engel S, Thaa B, Scolari S, Herrmann A. Lipid domain association of influenza virus proteins detected by dynamic fluorescence microscopy techniques. Cell Microbiol. 2013;15:179-89 pubmed publisher
    ..Finally, it is described how the signals that govern domain association in transfected cells affect replication of influenza virus. ..
  4. Veit M, Matczuk A, Sinhadri B, Krause E, Thaa B. Membrane proteins of arterivirus particles: structure, topology, processing and function. Virus Res. 2014;194:16-36 pubmed publisher
    ..This article reviews the molecular mechanisms of these cellular processes. Based on this, we present hypotheses on the structure and variability of arteriviral membrane proteins and their role during virus entry and budding. ..
  5. Brett K, Kordyukova L, Serebryakova M, Mintaev R, Alexeevski A, Veit M. Site-specific S-acylation of influenza virus hemagglutinin: the location of the acylation site relative to the membrane border is the decisive factor for attachment of stearate. J Biol Chem. 2014;289:34978-89 pubmed publisher
    ..Thus, the location of an acylation site relative to the transmembrane span is the main signal for stearate attachment, but the sequence context and the cell type modulate the fatty acid pattern. ..
  6. Wang M, Veit M. Hemagglutinin-esterase-fusion (HEF) protein of influenza C virus. Protein Cell. 2016;7:28-45 pubmed publisher
    ..Finally, we describe the functions of HEF: receptor binding, esterase activity and membrane fusion. ..
  7. Veit M, Siche S. S-acylation of influenza virus proteins: Are enzymes for fatty acid attachment promising drug targets?. Vaccine. 2015;33:7002-7 pubmed publisher
    ..We argue here that these DHHC-proteins might be promising drug targets since their blockade should result in suppression of viral replication, while acylation of cellular proteins will not be (or very little) compromised. ..
  8. Zhang M, Krabben L, Wang F, Veit M. Glycoprotein 3 of Porcine Reproductive and Respiratory Syndrome Virus Exhibits an Unusual Hairpin-Like Membrane Topology. J Virol. 2018;92: pubmed publisher
    ..Interestingly, PRRSV-1 strains secrete more GP3 than PRRSV-2. We speculate that secreted GP3 plays a role during PRRSV infection of pigs: it might serve as a decoy to distract antibodies away from virus particles. ..
  9. Siche S, Brett K, Möller L, Kordyukova L, Mintaev R, Alexeevski A, et al. Two Cytoplasmic Acylation Sites and an Adjacent Hydrophobic Residue, but No Other Conserved Amino Acids in the Cytoplasmic Tail of HA from Influenza A Virus Are Crucial for Virus Replication. Viruses. 2015;7:6458-75 pubmed publisher

More Information


  1. Matczuk A, Veit M. Signal peptide cleavage from GP3 enabled by removal of adjacent glycosylation sites does not impair replication of equine arteritis virus in cell culture, but the hydrophobic C-terminus is essential. Virus Res. 2014;183:107-11 pubmed publisher
    ..The data support our model that the signal peptide is exposed to the lumen of the ER and the C-terminus peripherally attaches GP3 to membranes. ..
  2. Thaa B, Siche S, Herrmann A, Veit M. Acylation and cholesterol binding are not required for targeting of influenza A virus M2 protein to the hemagglutinin-defined budozone. FEBS Lett. 2014;588:1031-6 pubmed publisher
    ..The motifs are thus irrelevant for M2 targeting in cells. ..