Recent Publications on Influenza virus

Hu B, Höfer CT, Thiele C, Veit M. Cholesterol binding to the transmembrane region of a group 2 HA of Influenza virus is essential for virus replication affecting both virus assembly and HA's fusion activity. J Virol. 2019 May 22. pii: JVI.00555-19. doi: 10.1128/JVI.00555-19.

Zhang W, Zhang L, He W, Zhang X, Wen B, Wang C, Xu Q, Li G, Zhou J, Veit M, Su S. Genetic Evolution and Molecular Selection of the HE Gene of Influenza C Virus. Viruses. 2019 Feb 19;11(2). pii: E167. doi: 10.3390/v11020167.

Su S, Fu X, Li G, Kerlin F, Veit M. Novel Influenza D virus: Epidemiology, pathology, evolution and biological characteristics. Virulence. 2017 Nov17;8(8):1580-1591. doi: 10.1080/21505594.2017.1365216. Review.

Höfer CT, Jolmes F, Haralampiev I, Veit M, Herrmann A. Influenza A virus nucleoprotein targets subnuclear structures. Cell Microbiol. 2017 Apr;19(4). doi: 10.1111/cmi.12679.

Siche S, Brett K, Möller L, Kordyukova LV, Mintaev RR, Alexeevski AV, Veit M. 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 AreCrucial for Virus Replication. Viruses. 2015 Dec 8;7(12):6458-75. doi:10.3390/v7122950.

Wang M, Ludwig K, Böttcher C, Veit M. The role of stearate attachment to the hemagglutinin-esterase-fusion glycoprotein HEF of influenza C virus. Cell Microbiol. 2016 May;18(5):692-704. doi: 10.1111/cmi.12541.

Veit M, Siche S. S-acylation of influenza virus proteins: Are enzymes for fatty acid attachment promising drug targets? Vaccine. 2015 Dec 8;33(49):7002-7. doi: 10.1016/j.vaccine.2015.08.095.

Scolari S, Imkeller K, Jolmes F, Veit M, Herrmann A, Schwarzer R. Modulation of cell surface transport and lipid raft localization by the cytoplasmic tail of the influenza virus hemagglutinin. Cell Microbiol. 2016 Jan;18(1):125-36. doi: 10.1111/cmi.12491.

Wang M, Veit M. Hemagglutinin-esterase-fusion (HEF) protein of influenza C virus. Protein Cell. 2016 Jan;7(1):28-45. doi: 10.1007/s13238-015-0193-x. Review.

Brett K, Kordyukova LV, Serebryakova MV, Mintaev RR, Alexeevski AV, 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 Dec 12;289(50):34978-89. doi: 10.1074/jbc.M114.586180.

de Vries M, Herrmann A, Veit M. A cholesterol consensus motif is required for efficient intracellular transport and raft association of a group 2 HA from influenza virus. Biochem J. 2015 Jan 15;465(2):305-14. doi: 10.1042/BJ20141114.

Mair CM, Meyer T, Schneider K, Huang Q, Veit M, Herrmann A. A histidine residue of the influenza virus hemagglutinin controls the pH dependence of the conformational change mediating membrane fusion. J Virol. 2014 Nov;88(22):13189-200. doi: 10.1128/JVI.01704-14..

Schmitt FJ, Thaa B, Junghans C, Vitali M, Veit M, Friedrich T. eGFP-pHsens as a highly sensitive fluorophore for cellular pH determination by fluorescence lifetime imaging microscopy (FLIM). Biochim Biophys Acta. 2014 Sep;1837(9):1581-93. doi: 10.1016/j.bbabio.2014.04.003.

Kummer S, Flöttmann M, Schwanhäusser B, Sieben C, Veit M, Selbach M, Klipp E, Herrmann A. Alteration of protein levels during influenza virus H1N1 infection in host cells: a proteomic survey of host and virus reveals differential dynamics. PLoS One. 2014 Apr 9;9(4):e94257. doi: 10.1371/journal.pone.0094257.

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 Mar 18;588(6):1031-6. doi: 10.1016/j.febslet.2014.02.014.

Mineev KS, Lyukmanova EN, Krabben L, Serebryakova MV, Shulepko MA, Arseniev AS, Kordyukova LV, Veit M. Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide. Protein Eng Des Sel. 2013 Sep;26(9):547-52. doi: 10.1093/protein/gzt034.

Veit M, Serebryakova MV, Kordyukova LV. Palmitoylation of influenza virus proteins. Biochem Soc Trans. 2013 Feb 1;41(1):50-5. doi: 10.1042/BST20120210. Review.

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 Feb;15(2):179-89. doi: 10.1111/cmi.12045

Serebryakova MV, Kordyukova LV, Rudneva IA, Kropotkina EA, Veit M, Baratova LA. Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin. Arch Virol. 2013 Feb;158(2):467-72. doi: 10.1007/s00705-012-1510-9

Veit M. Palmitoylation of virus proteins. Biol Cell. 2012 Sep;104(9):493-515. doi: 10.1111/boc.201200006. Review.

Veit M, Thaa B. Association of influenza virus proteins with membrane rafts. Adv Virol. 2011; 2011:370606. doi: 10.1155/2011/370606. Review

Engel S, de Vries M, Herrmann A, Veit M. Mutation of a raft-targeting signal in the transmembrane region retards transport of influenza virus hemagglutinin through the Golgi. FEBS Lett. 2012 Feb 3;586(3):277-82. doi: 10.1016/j.febslet.2012.01.002.

Thaa B, Tielesch C, Möller L, Schmitt AO, Wolff T, Bannert N, Herrmann A, Veit M. Growth of influenza A virus is not impeded by simultaneous removal of the cholesterol-binding and acylation sites in the M2 protein. J Gen Virol. 2012 Feb;93(Pt 2):282-92. doi: 10.1099/vir.0.038554-0.

Serebryakova MV, Kordyukova LV, Semashko TA, Ksenofontov AL, Rudneva IA, Kropotkina EA, Filippova IY, Veit M, Baratova LA. Influenza virus hemagglutinin spike neck architectures and interaction with model enzymes evaluated by MALDI-TOF mass spectrometry and bioinformatics tools. Virus Res. 2011 Sep;160(1-2):294-304. doi: 10.1016/j.virusres.2011.07.002.

Thaa B, Levental I, Herrmann A, Veit M. Intrinsic membrane association of the cytoplasmic tail of influenza virus M2 protein and lateral membrane sorting regulated by cholesterol binding and palmitoylation. Biochem J. 2011 Aug 1;437(3):389-97. doi: 10.1042/BJ20110706.

Kordyukova LV, Serebryakova MV, Polyansky AA, Kropotkina EA, Alexeevski AV, Veit M, Efremov RG, Filippova IY, Baratova LA. Linker and/or transmembrane regions of influenza A/Group-1, A/Group-2, and type B virus hemagglutinins are packed differently within trimers. Biochim Biophys Acta. 2011 Jul;1808(7):1843-54. doi: 10.1016/j.bbamem.2011.03.005.

Thaa B, Herrmann A, Veit M. Intrinsic cytoskeleton-dependent clustering of influenza virus M2 protein with hemagglutinin assessed by FLIM-FRET. J Virol. 2010 Dec;84(23):12445-9. doi: 10.1128/JVI.01322-10.

Nikolaus J, Scolari S, Bayraktarov E, Jungnick N, Engel S, Pia Plazzo A, Stöckl M, Volkmer R, Veit M, Herrmann A. Hemagglutinin of influenza virus partitions into the nonraft domain of model membranes. Biophys J. 2010 Jul 21;99(2):489-98. doi: 10.1016/j.bpj.2010.04.027.

Thaa B, Hofmann KP, Veit M. Viruses as vesicular carriers of the viral genome: a functional module perspective. Biochim Biophys Acta. 2010 Apr;1803(4):507-19. doi: 10.1016/j.bbamcr.2010.01.011. Review.

Kordyukova LV, Serebryakova MV, Baratova LA, Veit M. Site-specific attachment of palmitate or stearate to cytoplasmic versus transmembrane cysteines is a common feature of viral spike proteins. Virology. 2010 Mar 1;398(1):49-56. doi: 10.1016/j.virol.2009.11.039.

Engel S, Scolari S, Thaa B, Krebs N, Korte T, Herrmann A, Veit M. FLIM-FRET and FRAP reveal association of influenza virus haemagglutinin with membrane rafts. Biochem J. 2010 Jan 15;425(3):567-73. doi: 10.1042/BJ20091388.

Scolari S, Engel S, Krebs N, Plazzo AP, De Almeida RF, Prieto M, Veit M, Herrmann A. Lateral distribution of the transmembrane domain of influenza virus hemagglutinin revealed by time-resolved fluorescence imaging. J Biol Chem. 2009 Jun 5;284(23):15708-16. doi: 10.1074/jbc.M900437200.

Thaa B, Herrmann A, Veit M. The polybasic region is not essential for membrane binding of the matrix protein M1 of influenza virus. Virology. 2009 Jan 5;383(1):150-5. doi: 10.1016/j.virol.2008.10.001.

Kordyukova LV, Serebryakova MV, Baratova LA, Veit M. S acylation of the hemagglutinin of influenza viruses: mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine. J Virol. 2008 Sep;82(18):9288-92. doi: 10.1128/JVI.00704-08.

 

Recent Publications on Arteriviruses:

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 Jul 17;92(15). pii: e00660-18. doi: 10.1128/JVI.00660-18.

Zhang M, Veit M. Differences in signal peptide processing between GP3 glycoproteins of Arteriviridae. Virology. 2018 Apr;517:69-76. doi:10.1016/j.virol.2017.11.026.

Thaa B, Kaufer S, Neumann SA, Peibst B, Nauwynck H, Krause E, Veit M. The complex co-translational processing of glycoprotein GP5 of type 1 porcine reproductive and respiratory syndrome virus. Virus Res. 2017 Aug 15;240:112-120. doi: 10.1016/j.virusres.2017.08.004.

Matczuk AK, 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 Apr;183:107-11. doi: 10.1016/j.virusres.2014.02.005.

Veit M, Matczuk AK, Sinhadri BC, Krause E, Thaa B. Membrane proteins of arterivirus particles: structure, topology, processing and function. Virus Res. 2014 Dec 19;194:16-36. doi: 10.1016/j.virusres.2014.09.010. Review.

Thaa B, Sinhadri BC, Tielesch C, Krause E, Veit M. Signal peptide cleavage from GP5 of PRRSV: a minor fraction of molecules retains the decoy epitope, a presumed molecular cause for viral persistence. PLoS One. 2013 Jun 6;8(6):e65548. doi: 10.1371/journal.pone.0065548

Matczuk AK, Kunec D, Veit M. Co-translational processing of glycoprotein 3 from equine arteritis virus: N-glycosylation adjacent to the signal peptide prevents cleavage. J Biol Chem. 2013 Dec 6;288(49):35396-405. doi:10.1074/jbc.M113.505420.

Kabatek A, Veit M. Folding and oligomerization of the gp2b/gp3/gp4 spike proteins of equine arteritis virus in vitro. Viruses. 2012 Mar;4(3):414-23. doi: 10.3390/v4030414.

Thaa B, Kabatek A, Zevenhoven-Dobbe JC, Snijder EJ, Herrmann A, Veit M. Myristoylation of the arterivirus E protein: the fatty acid modification is not essential for membrane association but contributes significantly to virus infectivity. J Gen Virol. 2009 Nov;90(Pt 11):2704-12. doi:10.1099/vir.0.011957-0.

 

Other viruses:

He W, Auclert LZ, Zhai X, Wong G, Zhang C, Zhu H, Xing G, Wang S, He W, Li K, Wang L, Han GZ, Veit M, Zhou J, Su S. Interspecies Transmission, Genetic Diversity, and Evolutionary Dynamics of Pseudorabies Virus. J Infect Dis. 2019 May 5;219(11):1705-1715. doi: 10.1093/infdis/jiy731.

Gelhaus S, Thaa B, Eschke K, Veit M, Schwegmann-Weßels C. Palmitoylation of the Alphacoronavirus TGEV spike protein S is essential for incorporation into virus-like particles but dispensable for S-M interaction. Virology. 2014 Sep;464-465:397-405. doi: 10.1016/j.virol.2014.07.035.

Schwarzer R, Levental I, Gramatica A, Scolari S, Buschmann V, Veit M, Herrmann A. The cholesterol-binding motif of the HIV-1 glycoprotein gp41 regulates lateral sorting and oligomerization. Cell Microbiol. 2014 Oct;16(10):1565-81. doi: 10.1111/cmi.12314