Role of the Arginine Cluster in the Disordered Domain of Herpes Simplex Virus 1 UL34 for the Recruitment of ESCRT-III for Viral Primary Envelopment

Author:

Arii Jun1234ORCID,Takeshima Kosuke12,Maruzuru Yuhei123,Koyanagi Naoto123,Nakayama Yoshitaka1,Kato Akihisa123,Mori Yasuko4ORCID,Kawaguchi Yasushi123ORCID

Affiliation:

1. Division of Molecular Virology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan

2. Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan

3. Research Center for Asian Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan

4. Division of Clinical Virology, Center for Infectious Diseases, Kobe University Graduate School of Medicine, Kobe, Hyogo, Japan

Abstract

Herpesvirus UL34 homologs contain conserved amino-terminal domains that mediate vesicle formation through interactions with UL31 homologs during primary envelopment. UL34 homologs also comprise other domains adjacent to their membrane-anchoring regions, which differ in length, are variable in herpesviruses, and do not form distinguished secondary structures.

Funder

Japan Agency for Medical Research and Development

Ministry of Education, Culture, Sports, Science and Technology

Mitsubishi Foundation

Takeda Science Foundation

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference64 articles.

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2. Roizman B, Knipe DM, Whitley RJ. 2013. Herpes simplex viruses, p 1823–1897. In Knipe DM, Howley PM, Cohen JI, Griffin DE, Lamb RA, Martin MA, Racaniello VR, Roizman B (ed), Fields virology, 6th ed. Lippincott-Williams &Wilkins, Philadelphia, PA.

3. Herpesviruses remodel host membranes for virus egress

4. Vesicular Nucleo-Cytoplasmic Transport—Herpesviruses as Pioneers in Cell Biology

5. U L 31 and U L 34 Proteins of Herpes Simplex Virus Type 1 Form a Complex That Accumulates at the Nuclear Rim and Is Required for Envelopment of Nucleocapsids

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