Frontiers in Molecular Biosciences (Jul 2021)

PPI-MASS: An Interactive Web Server to Identify Protein-Protein Interactions From Mass Spectrometry-Based Proteomics Data

  • Mariela González-Avendaño,
  • Mariela González-Avendaño,
  • Simón Zúñiga-Almonacid,
  • Simón Zúñiga-Almonacid,
  • Simón Zúñiga-Almonacid,
  • Ian Silva,
  • Ian Silva,
  • Boris Lavanderos,
  • Boris Lavanderos,
  • Felipe Robinson,
  • Felipe Robinson,
  • Roberto Rosales-Rojas,
  • Roberto Rosales-Rojas,
  • Fabio Durán-Verdugo,
  • Wendy González,
  • Wendy González,
  • Mónica Cáceres,
  • Mónica Cáceres,
  • Oscar Cerda,
  • Oscar Cerda,
  • Ariela Vergara-Jaque,
  • Ariela Vergara-Jaque

DOI
https://doi.org/10.3389/fmolb.2021.701477
Journal volume & issue
Vol. 8

Abstract

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Mass spectrometry-based proteomics methods are widely used to identify and quantify protein complexes involved in diverse biological processes. Specifically, tandem mass spectrometry methods represent an accurate and sensitive strategy for identifying protein-protein interactions. However, most of these approaches provide only lists of peptide fragments associated with a target protein, without performing further analyses to discriminate physical or functional protein-protein interactions. Here, we present the PPI-MASS web server, which provides an interactive analytics platform to identify protein-protein interactions with pharmacological potential by filtering a large protein set according to different biological features. Starting from a list of proteins detected by MS-based methods, PPI-MASS integrates an automatized pipeline to obtain information of each protein from freely accessible databases. The collected data include protein sequence, functional and structural properties, associated pathologies and drugs, as well as location and expression in human tissues. Based on this information, users can manipulate different filters in the web platform to identify candidate proteins to establish physical contacts with a target protein. Thus, our server offers a simple but powerful tool to detect novel protein-protein interactions, avoiding tedious and time-consuming data postprocessing. To test the web server, we employed the interactome of the TRPM4 and TMPRSS11a proteins as a use case. From these data, protein-protein interactions were identified, which have been validated through biochemical and bioinformatic studies. Accordingly, our web platform provides a comprehensive and complementary tool for identifying protein-protein complexes assisting the future design of associated therapies.

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