ArticleVirus genes2015
Scylla serrata reovirus p35 protein expressed in Escherichia coli cells alters membrane permeability.
Article in Virus genes, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
The trial behind it
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Comparative Genomics of Viral Genomes and Identification of Three Novel Viroporin-Like Superfamilies.Microbial physiology · 2026Article
- NS2A comprises a putative viroporin of Dengue virus 2.Virulence · 2017Article
- Identification and characterization of host cell proteins interacting with Scylla serrata reovirus non-structural protein p35.Virus genes · 2017Article
- Identification and RNA segment assignment of six structural proteins of Scylla serrata reovirus.Virus genes · 2016Article
- Recombinant Dengue virus protein NS2B alters membrane permeability in different membrane models.Virology journal · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To promote viral entry, replication, release, and spread to neighboring cells, many cytolytic animal viruses encode proteins responsible for modification of host cell membrane permeability and for formation of ion channels in host cell membranes. Scylla serrata reovirus (SsRV) is a major pathogen that can severely damage mud crab (S. serrata) aquaculture. Protein p35, which is encoded by segment 10 of SsRV, contains two transmembrane domains. In this study, we found that SsRV p35 can induce membrane permeability changes when expressed in Escherichia coli. SsRV p35 expressed in bacterial cells existed as monomers under reducing conditions but formed homodimers and homotrimers under non-reducing conditions. These findings demonstrate that p35 may act as a viroporin; further studies are needed to elucidate the detailed structure-function relationships of this protein.
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Registered trials
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.