Acid phosphatase 2 (ACP2) is required for membrane fusion duringinfluenza virus entry

Collection with item attached
2017
Item details URL
http://open-repository.kisti.re.kr/cube/handle/open_repository/474210.do
DOI
10.1038/srep43893
Title
Acid phosphatase 2 (ACP2) is required for membrane fusion duringinfluenza virus entry
Description
We would like to thank Prof. Adolfo Garcia-Sastre (Mount Sinai School ofMedicine, New York, USA) for kindly providing the influenza A rPR8-GFPvirus. We thank Dr. Yohei Yamauch (ETH Zurich, Zurich, Switzerland) forkindly offering the monoclonal antibody A1. We also thank Prof. Young KiChoi (Chungbuk National University, Cheongju, South Korea) for kindlyproviding the H7 subtype AIVs. We are grateful to Dr. Thomas Hoenen(National Institute of Allergy and Infectious Diseases, MT, USA) forkindly sharing the Ebola trVLP system. We appreciate to Prof. Jens Bukh(University of Copenhagen and Hvidovre hospital, Hvidovre, Denmark) forproviding the HCV reporter virus. This study was supported by a grant ofthe TEPIK (Transgovernmental Enterprise for Pandemic Influenza inKorea), which is part of the Korea Healthcare Technology R&D Project bythe Ministry of Health & Welfare, Republic of Korea (Grant No.:A103001), as well as the Bio & Medical Technology Development Program ofthe NRF funded by the Korean government, MSIP (NRF-2013M3A9B5076486).
abstract
Influenza viruses exploit host factors to successfully replicate in infected cells. Using small interfering RNA (siRNA) technology, we identified six human genes required for influenza A virus (IAV) replication. Here we focused on the role of acid phosphatase 2 (ACP2), as its knockdown showed the greatest inhibition of IAV replication. In IAV-infected cells, depletion of ACP2 resulted in a significant reduction in the expression of viral proteins and mRNA, and led to the attenuation of virus multi-cycle growth. ACP2 knockdown also decreased replication of seasonal influenza A and B viruses and avian IAVs of the H7 subtype. Interestingly, ACP2 depletion had no effect on the replication of Ebola or hepatitis C virus. Because ACP2 is known to be a lysosomal acid phosphatase, we assessed the role of ACP2 in influenza virus entry. While neither binding of the viral particle to the cell surface nor endosomal acidification was affected in ACP2-depleted cells, fusion of the endosomal and viral membranes was impaired. As a result, downstream steps in viral entry were blocked, including nucleocapsid uncoating and nuclear import of viral ribonucleoproteins. Our results established ACP2 as a necessary host factor for regulating the fusion step of influenza virus entry.
provenance
Made available in Cube on 2018-09-28T10:40:05Z (GMT). No. of bitstreams: 0
language
English
author
Lee, Jihye
Kim, Jinhee
Son, Kidong
d'Orengiani, Anne-Laure Pham Humg d'Alexandry
Min, Ji-Young
accessioned
2018-09-28T10:40:05Z
available
2018-09-28T10:40:05Z
issued
2017
citation
SCIENTIFIC REPORTS(7)
issn
2045-2322
uri
http://open-repository.kisti.re.kr/cube/handle/open_repository/474210.do
Funder
미래창조과학부
Funding Program
바이오.의료기술개발
Project ID
1711037261
Jurisdiction
Rep.of Korea
Project Name
Development of next-generation influenza therapeutic agents
rights
openAccess
type
article


Files in This Item

There are no attached files.