MARCH8 Targets Cytoplasmic Lysine Residues of Various Viral Envelope Glycoproteins
Yanzhao Zhang, Seiya Ozono, Takuya Tada, Minoru Tobiume, Masanori Kameoka, Satoshi Kishigami, Hideaki Fujita, Kenzo Tokunaga
Abstract
A member of the MARCH E3 ubiquitin ligase family, MARCH8, downregulates many different kinds of host transmembrane proteins, resulting in the regulation of cellular homeostasis. On the other hands, MARCH8 acts as an antiviral factor when it binds to and downregulates HIV-1 envelope glycoprotein and vesicular stomatitis virus G-glycoprotein that are viral transmembrane proteins. This study reveals that, as in the case of cellular membrane proteins, MARCH8 shows broad-spectrum inhibition against various viral envelope glycoproteins by recognizing their cytoplasmic lysine residues, resulting in lysosomal degradation.
Topics & Concepts
GlycoproteinLysineEnvelope (radar)CytoplasmBiologyChemistryBiochemistryCell biologyVirologyComputational biologyComputer scienceAmino acidRadarTelecommunicationsVirus-based gene therapy researchinterferon and immune responsesViral gastroenteritis research and epidemiology