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Related Concept Videos

Protein Networks02:26

Protein Networks

4.7K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Updated: Apr 16, 2026

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
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A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

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Host-pathogen interaction profiling using self-assembling human protein arrays.

Xiaobo Yu1, Kimberly B Decker2, Kristi Barker1

  • 1†Virginia G. Piper Center for Personalized Diagnostics, Biodesign Institute, Arizona State University, Tempe, Arizona 85287, United States.

Journal of Proteome Research
|March 6, 2015
PubMed
Summary
This summary is machine-generated.

We developed a new protein interaction detection method to study host-pathogen interactions. This approach identified novel targets for Legionella pneumophila effectors, advancing our understanding of microbial infections.

Keywords:
AMPylationLidARab1SidMinteractomenucleic acid programmable protein array (NAPPA)

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Host-pathogen protein interactions are crucial in infections but difficult to study.
  • Existing methods for identifying these interactions have limitations, including abundance biases and lack of experimental flexibility.

Purpose of the Study:

  • To develop and apply a novel, bias-free protein interaction detection platform for studying host-pathogen protein networks.
  • To identify interaction partners and substrates of Legionella pneumophila effectors SidM and LidA.

Main Methods:

  • Utilized the Nucleic Acid-Programmable Protein Array (NAPPA) platform combined with a HaloTag-Halo ligand detection system.
  • Screened interactions between L. pneumophila effectors (SidM, LidA) and approximately 10,000 human proteins.
  • Employed Click chemistry-based NAPPA to identify substrates for SidM's AMPylation activity.
  • Validated novel targets using in vitro pull-down and in vivo cell-based assays.

Main Results:

  • Identified known and novel interaction candidates for L. pneumophila SidM and LidA effectors.
  • Discovered substrates for SidM's AMPylation activity.
  • Confirmed a subset of novel targets through independent validation experiments.
  • Gained insights into effector discrimination of host Rab GTPases.

Conclusions:

  • The NAPPA-HaloTag system offers a robust, high-throughput method for identifying host-pathogen protein interactions and effector substrates.
  • This platform circumvents protein purification and labeling requirements, making it broadly applicable to various pathogens.
  • The findings provide a deeper understanding of L. pneumophila pathogenesis and host manipulation strategies.