Enriching the viral-host interactomes with interactions mediated by SH3 domains

Amino Acids. 2010 May;38(5):1541-7. doi: 10.1007/s00726-009-0375-z. Epub 2009 Nov 2.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviridae / pathogenicity
  • Amino Acid Sequence
  • Host-Pathogen Interactions*
  • Humans
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • src Homology Domains*