ArticleVirus research2010
Identification of cellular proteins interacting with equine infectious anemia virus S2 protein.
Article in Virus research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Review
- TIM-mediated inhibition of HIV-1 release is antagonized by Nef but potentiated by SERINC proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- S2 from equine infectious anemia virus is an infectivity factor which counteracts the retroviral inhibitors SERINC5 and SERINC3.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A unique evolution of the s2 gene of equine infectious anemia virus in hosts correlated with particular infection statuses.Viruses · 2014Article
- Bcl-2-associated transcription factor 1 interacts with fragile X-related protein 1.Acta biochimica et biophysica Sinica · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The macrophage-tropic lentivirus, equine infectious anemia virus (EIAV), encodes the small auxiliary protein S2 from a short open reading frame that overlaps the amino terminus of env EIAV S2 is dispensable for virus replication in cultured cells but is required for disease production. S2 is approximately 7 kDa and has no overall amino acid sequence homology to other cellular or viral proteins. Therefore it is likely that S2 plays a role as an adaptor protein. To further investigate S2 function we performed a yeast-2-hybrid screen to identify cellular proteins that interact with EIAV S2. The screen identified two human cellular proteins, amplified in osteosarcoma (OS-9) and proteasome 26S ATPase subunit 3 (PSMC3) that interact with S2. The equine homologues of these proteins were cloned and their interactions with S2 confirmed using co-immunoprecipitation assays. We identified two OS-9 isoforms that interact with S2 and a third splice variant that does not, indicating a region of OS-9 apparently required for the S2 interaction. The roles of these cellular proteins during EIAV infection have not been determined.
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Registered trials
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