MARCH8 Targets Cytoplasmic Lysine Residues of Various Viral Envelope Glycoproteins-Reference-Cited by-同舟云学术

MARCH8 Targets Cytoplasmic Lysine Residues of Various Viral Envelope Glycoproteins

Published:2022-02-23 Issue:1 Volume:10 Page:
ISSN:2165-0497
Container-title:Microbiology Spectrum
language:en
Short-container-title:Microbiol Spectr

Author:

Zhang Yanzhao¹^ORCID,Ozono Seiya¹²^ORCID,Tada Takuya¹³^ORCID,Tobiume Minoru¹^ORCID,Kameoka Masanori⁴^ORCID,Kishigami Satoshi²^ORCID,Fujita Hideaki⁵^ORCID,Tokunaga Kenzo¹^ORCID

Affiliation:

1. Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan

2. Faculty of Life and Environmental Sciences, University of Yamanashi, Yamanashi, Japan

3. Department of Microbiology, New York University School of Medicine, New York, New York, USA

4. Department of Public Health, Kobe University Graduate School of Health Sciences, Hyogo, Japan

5. Faculty of Pharmaceutical Sciences, Nagasaki International University, Nagasaki, Japan

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.

Funder

Japan Agency for Medical Research and Development

MEXT | Japan Society for the Promotion of Science

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Cell Biology,Microbiology (medical),Genetics,General Immunology and Microbiology,Ecology,Physiology

Link

https://journals.asm.org/doi/pdf/10.1128/spectrum.00618-21

Reference30 articles.

1. Downregulation of Major Histocompatibility Complex Class I by Human Ubiquitin Ligases Related to Viral Immune Evasion Proteins

2. c-MIR, a Human E3 Ubiquitin Ligase, Is a Functional Homolog of Herpesvirus Proteins MIR1 and MIR2 and Has Similar Activity