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The protein–protein interaction map of Helicobacter pylori

Author

Listed:
  • 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)

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.

Suggested Citation

  • 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 Labi, 2001. "The protein–protein interaction map of Helicobacter pylori," Nature, Nature, vol. 409(6817), pages 211-215, January.
    • Handle: RePEc:nat:nature:v:409:y:2001:i:6817:d:10.1038_35051615
    DOI: 10.1038/35051615
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    Cited by:

    1. Shihui Chen & Carolyn M. Phillips, 2024. "HRDE-2 drives small RNA specificity for the nuclear Argonaute protein HRDE-1," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    2. Erica W. Carter & Orlene Guerra Peraza & Nian Wang, 2023. "The protein interactome of the citrus Huanglongbing pathogen Candidatus Liberibacter asiaticus," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Haley E. Adcox & Jason R. Hunt & Paige E. Allen & Thomas E. Siff & Kyle G. Rodino & Andrew K. Ottens & Jason A. Carlyon, 2024. "Orientia tsutsugamushi Ank5 promotes NLRC5 cytoplasmic retention and degradation to inhibit MHC class I expression," Nature Communications, Nature, vol. 15(1), pages 1-21, December.
    4. Julian Petersen & Lukas Englmaier & Artem V. Artemov & Irina Poverennaya & Ruba Mahmoud & Thibault Bouderlique & Marketa Tesarova & Ruslan Deviatiiarov & Anett Szilvásy-Szabó & Evgeny E. Akkuratov & D, 2023. "A previously uncharacterized Factor Associated with Metabolism and Energy (FAME/C14orf105/CCDC198/1700011H14Rik) is related to evolutionary adaptation, energy balance, and kidney physiology," Nature Communications, Nature, vol. 14(1), pages 1-22, December.

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