The protein–protein interaction map of Helicobacter pylori
Jean-Christophe Rain,
Luc Selig,
Hilde De Reuse,
Véronique Battaglia,
Céline Reverdy,
Stéphane Simon,
Gerlinde Lenzen,
Fabien Petel,
Jérôme Wojcik,
Vincent Schächter,
Y. Chemama,
Agnès Labigne and
Pierre Legrain ()
Additional contact information
Jean-Christophe Rain: Hybrigenics SA
Luc Selig: Hybrigenics SA
Hilde De Reuse: Unité de Pathogénie Bactérienne des Muqueuses, Institut Pasteur
Véronique Battaglia: Hybrigenics SA
Céline Reverdy: Hybrigenics SA
Stéphane Simon: Hybrigenics SA
Gerlinde Lenzen: Hybrigenics SA
Fabien Petel: Hybrigenics SA
Jérôme Wojcik: Hybrigenics SA
Vincent Schächter: Hybrigenics SA
Y. Chemama: Hybrigenics SA
Agnès Labigne: Unité de Pathogénie Bactérienne des Muqueuses, Institut Pasteur
Pierre Legrain: Hybrigenics SA
Nature, 2001, vol. 409, issue 6817, 211-215
Abstract:
Abstract With the availability of complete DNA sequences for many prokaryotic and eukaryotic genomes, and soon for the human genome itself, it is important to develop reliable proteome-wide approaches for a better understanding of protein function1. As elementary constituents of cellular protein complexes and pathways, protein–protein interactions are key determinants of protein function. Here we have built a large-scale protein–protein interaction map of the human gastric pathogen Helicobacter pylori. We have used a high-throughput strategy of the yeast two-hybrid assay to screen 261 H. pylori proteins against a highly complex library of genome-encoded polypeptides2. Over 1,200 interactions were identified between H. pylori proteins, connecting 46.6% of the proteome. The determination of a reliability score for every single protein–protein interaction and the identification of the actual interacting domains permitted the assignment of unannotated proteins to biological pathways.
Date: 2001
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:409:y:2001:i:6817:d:10.1038_35051615
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DOI: 10.1038/35051615
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