Profiling the DuCV-1 Cap-associated host interactome by Co-IP/LC-MS: implications for host-response pathways and viral pathogenesis
- 1Institute of Animal Husbandry and Veterinary Medicine, Jiangxi Academy of Agricultural Sciences, Nanchang, 330200, China
- 2Jiangxi Provincial Key Laboratory of Green and Healthy Breeding of Livestock and Poultry, Nanchang, Jiangxi, 330200, China
- 3Jiangxi Biological Vocational College, Nanchang, Jiangxi, 330200, China
Abstract
Duck circovirus genotype 1 (DuCV-1) infection is a severe immunosuppressive disease that significantly impairs poultry growth. As the sole structural protein and major immunogen of DuCV-1, the capsid protein (Cap) plays a critical role in viral infection and pathogenesis. Elucidating the interactions between Cap and host proteins is essential for revealing the molecular basis of DuCV-1 pathogenicity. In this study, we performed, for the first time, using immunoprecipitation coupled with mass spectrometry (MS) to identify 288 potential host proteins that interact with Cap in Cap-transfected HD11 cells. Integrative analyses of protein–protein interaction (PPI) networks, Gene Ontology (GO) annotation, and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment showed that Cap-interacting host proteins are functionally enriched in multiple biological processes, including cytoskeleton remodeling, nucleic acid translation apparatus, endocytic trafficking, autophagy, and innate immune signaling. Further functional enrichment analyses confirmed that these Cap-binding factors are predominantly enriched in pathways associated with cytoskeleton remodeling, protein translation, transcriptional regulation, and DNA damage response. Moreover, we verified the binding of nine candidate Cap-interacting proteins to DuCV-1 Cap, including RB1-inducible coiled-coil 1, Exocyst complex component 1, Tubulin alpha-1A chain, Transcription factor E2F8, Nucleolar and coiled-body phosphoprotein 1, Ubiquitin-protein ligase E3B, DNA repair protein RAD52 homolog, Junction plakoglobin, and Tubulin alpha-1C chain. Collectively, the interactome dataset and network analysis provide new insights into the potential pathogenic mechanisms of DuCV-1.
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BibTeX
@article{lin2026profiling,
title = {{Profiling the DuCV-1 Cap-associated host interactome by Co-IP/LC-MS: implications for host-response pathways and viral pathogenesis}},
author = {Cui Lin and Jia Tan and Lengmei Wang and Chengcheng Wu and Fanfan Zhang and Na Li and Wenjing Song and Meifang Tan and Jiangnan Huang and Haiqin Li},
journal = {Poultry Science},
year = {2026},
month = oct,
doi = {10.1016/j.psj.2026.107946},
url = {https://doi.org/10.1016/j.psj.2026.107946},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - JOUR
TI - Profiling the DuCV-1 Cap-associated host interactome by Co-IP/LC-MS: implications for host-response pathways and viral pathogenesis
AU - Cui Lin
AU - Jia Tan
AU - Lengmei Wang
AU - Chengcheng Wu
AU - Fanfan Zhang
AU - Na Li
AU - Wenjing Song
AU - Meifang Tan
AU - Jiangnan Huang
AU - Haiqin Li
PY - 2026
DA - 2026/10/11
JO - Poultry Science
DO - 10.1016/j.psj.2026.107946
UR - https://doi.org/10.1016/j.psj.2026.107946
AB - Duck circovirus genotype 1 (DuCV-1) infection is a severe immunosuppressive disease that significantly impairs poultry growth. As the sole structural protein and major immunogen of DuCV-1, the capsid protein (Cap) plays a critical role in viral infection and pathogenesis. Elucidating the interactions between Cap and host proteins is essential for revealing the molecular basis of DuCV-1 pathogenicity. In this study, we performed, for the first time, using immunoprecipitation coupled with mass spectrometry (MS) to identify 288 potential host proteins that interact with Cap in Cap-transfected HD11 cells. Integrative analyses of protein–protein interaction (PPI) networks, Gene Ontology (GO) annotation, and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment showed that Cap-interacting host proteins are functionally enriched in multiple biological processes, including cytoskeleton remodeling, nucleic acid translation apparatus, endocytic trafficking, autophagy, and innate immune signaling. Further functional enrichment analyses confirmed that these Cap-binding factors are predominantly enriched in pathways associated with cytoskeleton remodeling, protein translation, transcriptional regulation, and DNA damage response. Moreover, we verified the binding of nine candidate Cap-interacting proteins to DuCV-1 Cap, including RB1-inducible coiled-coil 1, Exocyst complex component 1, Tubulin alpha-1A chain, Transcription factor E2F8, Nucleolar and coiled-body phosphoprotein 1, Ubiquitin-protein ligase E3B, DNA repair protein RAD52 homolog, Junction plakoglobin, and Tubulin alpha-1C chain. Collectively, the interactome dataset and network analysis provide new insights into the potential pathogenic mechanisms of DuCV-1.
SN - 0032-5791
SN - 1525-3171
ER -