Aarhus University Seal / Aarhus Universitets segl

Esben Meldgaard Høgh Quistgaard

Interaction between human BAP31 and respiratory syncytial virus small hydrophobic (SH) protein

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Yan Li, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
  • ,
  • Neeraj Jain, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
  • ,
  • Suweeraya Limpanawat, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
  • ,
  • Janet To, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
  • ,
  • Esben M Quistgaard
  • Par Nordlund, School of Biological Sciences, Nanyang Technological University, 637551, Singapore; Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
  • ,
  • Thirumaran Thanabalu, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
  • ,
  • Jaume Torres, School of Biological Sciences, Nanyang Technological University, 637551, Singapore. Electronic address: jtorres@ntu.edu.sg.

The small hydrophobic (SH) protein is a short channel-forming polypeptide encoded by the human respiratory syncytial virus (hRSV). Deletion of SH protein leads to the viral attenuation in mice and primates, and delayed apoptosis in infected cells. We have used a membrane-based yeast two-hybrid system (MbY2H) and a library from human lung cDNA to detect proteins that bind SH protein. This led to the identification of a membrane protein, B-cell associated protein 31 (BAP31). Transfected SH protein co-localizes with transfected BAP31 in cells, and pulls down endogenous BAP31. Titration of purified C-terminal endodomain of BAP31 against isotopically labeled SH protein in detergent micelles suggests direct interaction between the two proteins. Given the key role of BAP31 in protein trafficking and its critical involvement in pro- and anti-apoptotic pathways, this novel interaction may constitute a potential drug target.

Original languageEnglish
JournalVirology
Volume482
Pages (from-to)105-10
Number of pages6
ISSN0042-6822
DOIs
Publication statusPublished - Aug 2015
Externally publishedYes

    Research areas

  • Animals, Host-Pathogen Interactions, Humans, Membrane Proteins, Protein Binding, Protein Interaction Mapping, Respiratory Syncytial Virus, Human, Two-Hybrid System Techniques, Viral Proteins, Journal Article, Research Support, Non-U.S. Gov't

See relations at Aarhus University Citationformats

ID: 118858727