Skip to content
DraconiticResearch
Search Sources API
203,234 studies31 sourcesUpdated 41 min ago
Peer-reviewedCC BYBiophysics reports

Structure-based prediction reveals FAM105A as an African swine fever virus I215L interactor.

  • Xing Chen1
  • Danyang Zhang1
  • Yuxi Yang1
  • Fayu Yang1
  • Shilei Zhang1,2,3
  1. 1State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China.
  2. 2Gansu Province Research Center for Basic Disciplines of Pathogen Biology, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China.
  3. 3African Swine Fever Regional Laboratory of China, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China.
Read full textPDFDOICite

Abstract

African swine fever virus (ASFV) causes a fatal hemorrhagic disease in pigs, leading to severe economic losses worldwide. The viral ubiquitin-conjugating enzyme I215L (E2) is critical for ASFV replication and modulation of host antiviral responses. Host deubiquitinating enzymes (DUBs) bind to E2 enzymes to inhibit the transfer of ubiquitin. In this study, we systematically screened 34 swine DUBs using HDOCK docking and AlphaFold3 modeling, identifying FAM105A as the most probable interactor. Co-immunoprecipitation assay validated the interaction between I215L and FAM105A. Structural analyses revealed seven I215L residues (E19, N20, M99, S102, A104, D108, S116) that form defined polar contacts, among which M99, D108, and S116 are critical for binding stability. These findings identify FAM105A as a novel host target of ASFV I215L, establishing a new paradigm for studying viral-host protein interactions.

Related

  1. The DUF2439/RADIF domain of ZGRF1 is a RAD51 interactor and facilitator
    Oline Pade, Anita Brozkova, Anne Katrine Wrist Simonsen +13
    Cell ReportsPeer-reviewedCC BY 4.0General biologyCrossref
  2. COMPARATIVE PHENOMICS IN Limnospira platensis STRAINS REVEALS PHOTOBIOENERGETIC SIMILARITIES AND DIFFERENCES IN AMERICAN AND AFRICAN STRAINS
    M. Zavala, J. A. Perez-Loera, C. Peters +1
    bioRxivPreprintCC BY-NCFull textSystems & synthetic biologybioRxiv
  3. Personalized genomic landscape of prostate cancer in African American men reveals novel drivers and therapeutic opportunities
    Shanta Murthy, Katie Fago, James Knight +5
    PLOS OnePeer-reviewedCC BY 4.0Full textGenetics & genomicsOncologyPLOS
  4. A Highly Permissive K-C4 Cell Clone for Genotype II African Swine Fever Virus Reveals Passage-Dependent Hemadsorption Changes Associated with EP402R Deletion.
    Eun-Gyeong Lee, Ju-Hun Kim, Sarah Lim +8
    Veterinary sciencesPeer-reviewedCC BYFull textPlant biologyEurope PMC
  5. Dual‐Locus Metabarcoding Reveals Dry‐Season Dietary Differentiation Between Elephants and Impalas in a South African Savanna
    Kyle R. van Wyk, Danielle Botha, Sandra Barnard +1
    Ecology and evolutionPeer-reviewedCC BYFull textEcologyEurope PMCCrossref

Cite

BibTeXRIS
BibTeX
@article{chen2026structurebased,
  title = {{Structure-based prediction reveals FAM105A as an African swine fever virus I215L interactor.}},
  author = {Xing Chen and Danyang Zhang and Yuxi Yang and Fayu Yang and Shilei Zhang},
  journal = {Biophysics reports},
  year = {2026},
  month = oct,
  doi = {10.52601/bpr.2025.250057},
  url = {https://europepmc.org/article/MED/42997075},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Structure-based prediction reveals FAM105A as an African swine fever virus I215L interactor.
AU  - Xing Chen
AU  - Danyang Zhang
AU  - Yuxi Yang
AU  - Fayu Yang
AU  - Shilei Zhang
PY  - 2026
DA  - 2026/10/31
JO  - Biophysics reports
DO  - 10.52601/bpr.2025.250057
UR  - https://europepmc.org/article/MED/42997075
AB  - African swine fever virus (ASFV) causes a fatal hemorrhagic disease in pigs, leading to severe economic losses worldwide. The viral ubiquitin-conjugating enzyme I215L (E2) is critical for ASFV replication and modulation of host antiviral responses. Host deubiquitinating enzymes (DUBs) bind to E2 enzymes to inhibit the transfer of ubiquitin. In this study, we systematically screened 34 swine DUBs using HDOCK docking and AlphaFold3 modeling, identifying FAM105A as the most probable interactor. Co-immunoprecipitation assay validated the interaction between I215L and FAM105A. Structural analyses revealed seven I215L residues (E19, N20, M99, S102, A104, D108, S116) that form defined polar contacts, among which M99, D108, and S116 are critical for binding stability. These findings identify FAM105A as a novel host target of ASFV I215L, establishing a new paradigm for studying viral-host protein interactions.
SN  - 2364-3439
SN  - 2364-3420
ER  -