Evidence map›Paper›PMID 24807724›Full record

ArticleJournal of virology2014

Hijacking of host calreticulin is required for the white spot syndrome virus replication cycle.

Apiruck Watthanasurorot, Enen Guo, Sirinit Tharntada, Chu-Fang Lo, Kenneth Söderhäll, Irene Söderhäll

RetractedOpen access · bronzeAbstract readRetracted Publication
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

Apiruck WatthanasurorotDepartment of Comparative Physiology, Uppsala University, Uppsala, Sweden.
Enen GuoDepartment of Comparative Physiology, Uppsala University, Uppsala, Sweden.
Sirinit TharntadaDepartment of Veterinary Technology, Faculty of Veterinary Technology, Kasetsart University, Bangkok, Thailand.
Chu-Fang LoCollege of Bioscience and Biotechnology, National Cheng Kung University, Tainan, Taiwan, Republic of China.
Kenneth SöderhällDepartment of Comparative Physiology, Uppsala University, Uppsala, Sweden Science for Life Laboratory, Uppsala University, Uppsala, Sweden.
Irene SöderhällDepartment of Comparative Physiology, Uppsala University, Uppsala, Sweden Irene.Soderhall@ebc.uu.se.
Uppsala University · SEKasetsart University · THNational Cheng Kung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously shown that multifunctional calreticulin (CRT), which resides in the endoplasmic reticulum (ER) and is involved in ER-associated protein processing, responds to infection with white spot syndrome virus (WSSV) by increasing mRNA and protein expression and by forming a complex with gC1qR and thereby delaying apoptosis. Here, we show that CRT can directly interact with WSSV structural proteins, including VP15 and VP28, during an early stage of virus infection. The binding of VP28 with CRT does not promote WSSV entry, and CRT-VP15 interaction was detected in the viral genome in virally infected host cells and thus may have an effect on WSSV replication. Moreover, CRT was detected in the viral envelope of purified WSSV virions. CRT was also found to be of high importance for proper oligomerization of the viral structural proteins VP26 and VP28, and when CRT glycosylation was blocked with tunicamycin, a significant decrease in both viral replication and assembly was detected. Together, these findings suggest that CRT confers several advantages to WSSV, from the initial steps of WSSV infection to the assembly of virions. Therefore, CRT is required as a "vital factor" and is hijacked by WSSV for its replication cycle. Importance: White spot syndrome virus (WSSV) is a double-stranded DNA virus and the cause of a serious disease in a wide range of crustaceans that often leads to high mortality rates. We have previously shown that the protein calreticulin (CRT), which resides in the endoplasmic reticulum (ER) of the cell, is important in the host response to the virus. In this report, we show that the virus uses this host protein to enter the cell and to make the host produce new viral structural proteins. Through its interaction with two viral proteins, the virus "hijacks" host calreticulin and uses it for its own needs. These findings provide new insight into the interaction between a large DNA virus and the host protein CRT and may help in understanding the viral infection process in general.

Indexed as

Host-Pathogen InteractionsVirus ReplicationAnimalsAstacoideaCalreticulinCells, CulturedNucleocapsid ProteinsProtein BindingViral Envelope ProteinsVirus AssemblyWhite spot syndrome virus 1CalreticulinNucleocapsid ProteinsViral Envelope ProteinsVP15 protein, white spot syndrome virusVP28 protein, white spot syndrome virus

Identifiers

PMID24807724
PMCPMC4097763
OpenAlexW2159059720

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.