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Bioinformatics 2009 25(12):i259-1267; doi:10.1093/bioinformatics/btp196
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© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Global alignment of protein–protein interaction networks by graph matching methods

Mikhail Zaslavskiy 1,2,3, Francis Bach 4 and Jean-Philippe Vert 1,2,3,*

1Centre for Computational Biology, Mines ParisTech, 35 rue Saint-Honoré, Fontainebleau, F-77300, 2Institut Curie, 3INSERM, U900, Paris, F-75248 and 4INRIA-WILLOW project, Ecole Normale Supérieure, Paris, France

*To whom correspondence should be addressed.


  Abstract

Motivation: Aligning protein–protein interaction (PPI) networks of different species has drawn a considerable interest recently. This problem is important to investigate evolutionary conserved pathways or protein complexes across species, and to help in the identification of functional orthologs through the detection of conserved interactions. It is, however, a difficult combinatorial problem, for which only heuristic methods have been proposed so far.

Results: We reformulate the PPI alignment as a graph matching problem, and investigate how state-of-the-art graph matching algorithms can be used for that purpose. We differentiate between two alignment problems, depending on whether strict constraints on protein matches are given, based on sequence similarity, or whether the goal is instead to find an optimal compromise between sequence similarity and interaction conservation in the alignment. We propose new methods for both cases, and assess their performance on the alignment of the yeast and fly PPI networks. The new methods consistently outperform state-of-the-art algorithms, retrieving in particular 78% more conserved interactions than IsoRank for a given level of sequence similarity.

Availability: All data and codes are freely and publicly available upon request.

Contact: jean-philippe.vert{at}mines-paristech.fr


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