Abstract
Protein–protein interactions play an essential role in the regulation of most cellular processes. The process of viral infection is no exception and many viral pathogenic strategies involve targeting and perturbing host–protein interactions. The characterization of the host protein subnetworks disturbed by invading viruses is a major goal of viral research and may contribute to reveal fundamental biological mechanisms and to identify new therapeutic strategies. To assist in this approach, we have developed a database, VirusMINT, which stores in a structured format most of the published interactions between viral and host proteome. Although SH3 are the most ubiquitous and abundant class of protein binding modules, VirusMINT contains only a few interactions mediated by this domain class. To overcome this limitation, we have applied the whole interactome scanning experiment approach to identify interactions between 15 human SH3 domains and viral proline-rich peptides of two oncogenic viruses, human papillomavirus type 16 and human adenovirus A type 12. This approach identifies 114 new potential interactions between the human SH3 domains and proline-rich regions of the two viral proteomes.
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This work was supported by a grant from AIRC.
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M. Carducci and L. Licata should be regarded as joint first authors.
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Supplementary Table 1
. Regular expressions mapping the viral proline-rich peptides used in the screening. The “x” correspond to any amino acid residues. (XLS 30 kb)
Supplementary Table 2
. Viral proline-rich peptides. 46 viral peptides synthesized on cellulose membrane, belonging to Human Adenovirus A type 12 and Human Papilloma type 16 proteome (Column 1), viral protein name (column 2), Uniprot accession number (column 3), peptide sequences (column 4) and peptide ranges (column 5) are shown. (XLS 34 kb)
Supplementary Table 3
. Host-virus domain-peptide interactions. The 213 physical interaction found in the this screening are listed. Column 1 and 2 show the name of Human Protein (HP) and Viral Protein (VP). The following columns contain Uniprot accession number, viral peptides sequences, human SH3 domain ranges and viral pro-rich peptide ranges. (XLS 43 kb)
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Carducci, M., Licata, L., Peluso, D. et al. Enriching the viral–host interactomes with interactions mediated by SH3 domains. Amino Acids 38, 1541–1547 (2010). https://doi.org/10.1007/s00726-009-0375-z
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DOI: https://doi.org/10.1007/s00726-009-0375-z