Processing and Function of the Gp2/3/4 Spike of the Porcine Reproductive and Respiratory Syndrome Virus (PRRSV)

Applicant Privatdozent Dr. Michael Veit

Subject Area Veterinary Medical Science

Term from 2014 to 2020

Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 256219832

Final Report Year 2020

Final Report Abstract

No abstract available

(2014) 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. 183:107-11
Matczuk AK, Veit M
(See online at https://doi.org/10.1016/j.virusres.2014.02.005)
(2014) Membrane proteins of arterivirus particles: Structure, topology, processing and function. Virus Res. 194:16-36
Veit M, Matczuk AK, Sinhadri BC, Krause E, Thaa B
(See online at https://doi.org/10.1016/j.virusres.2014.09.010)
(2017) The complex co-translational processing of glycoprotein GP5 of type 1 porcine reproductive and respiratory syndrome virus. Virus Res. 240:112-120
Thaa B, Kaufer S, Neumann SA, Peibst B, Nauwynck H, Krause E, Veit M
(See online at https://doi.org/10.1016/j.virusres.2017.08.004)
(2018) Differences in signal peptide processing between GP3 glycoproteins of Arteriviridae. Virology. 517:69-76
Zhang M, Veit M
(See online at https://doi.org/10.1016/j.virol.2017.11.026)
(2018) Glycoprotein 3 of Porcine Reproductive and Respiratory Syndrome Virus Exhibits an Unusual Hairpin-Like Membrane Topology. J Virol. 17;92(15): e00660-18
Zhang M, Krabben L, Wang F, Veit M
(See online at https://doi.org/10.1128/JVI.00660-18)