Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.1K
Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
4.1K
Proteomics01:33

Proteomics

9.2K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
9.2K
Protein Networks02:26

Protein Networks

4.4K
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,...
4.4K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
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...
14.4K
Protein Organization01:24

Protein Organization

8.8K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
8.8K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Host interactomes of <i>Streptococcus oralis</i> and <i>Streptococcus gordonii</i> exposed to saliva or serum.

Microbiology spectrum·2026
Same author

Variants in human CD48 lead to impaired T cell immunity and increased inflammation.

The Journal of clinical investigation·2026
Same author

Rapid Proteome-Wide Discovery of Protein-Protein Interactions With ppIRIS.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Mapping targetable sites on the human surfaceome for the design of novel binders.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

DynamicGT: A dynamic-aware geometric transformer model to predict protein-binding interfaces in flexible and disordered regions.

Cell systems·2025
Same author

Commensal Peptoniphilus harei induce activation of monocytes via TLR2/CD14 signalling in whole blood.

Medical microbiology and immunology·2025

Related Experiment Video

Updated: Dec 28, 2025

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

48.7K

Structural proteomics, electron cryo-microscopy and structural modeling approaches in bacteria-human protein

Sounak Chowdhury1, Lotta Happonen1, Hamed Khakzad2,3,4

  • 1Division of Infection Medicine, Department of Clinical Sciences, Faculty of Medicine, Lund University, 22184, Lund, Sweden.

Medical Microbiology and Immunology
|February 20, 2020
PubMed
Summary

Understanding host-pathogen protein interactions is key in infection medicine. This review highlights how proteomics, cryo-electron microscopy, and structural modeling advance knowledge of these crucial interactions for drug development.

Keywords:
Affinity-purification mass spectrometryCross-linking mass spectrometryElectron cryo-microscopyHost–pathogen interactionMolecular modelingProteomics

More Related Videos

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.8K
Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

14.0K

Related Experiment Videos

Last Updated: Dec 28, 2025

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

48.7K
Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.8K
Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

14.0K

Area of Science:

  • Infection Medicine
  • Structural Biology
  • Proteomics

Background:

  • Host-pathogen protein-protein interactions are central to understanding infection mechanisms, including bacterial adhesion, spread, and survival.
  • Determining the structure and function of these interactions is a critical challenge in infection medicine.

Purpose of the Study:

  • To review how advanced techniques like proteomics, electron cryo-microscopy, and structural modeling enhance the study of host-pathogen interactions.
  • To showcase specific examples where affinity-purification (AP) and cross-linking (XL) mass spectrometry (MS) have elucidated these interactions.
  • To discuss future applications of these methods for drug and vaccine development.

Main Methods:

  • Affinity-purification (AP) and cross-linking (XL) mass spectrometry (MS).
  • Electron cryo-microscopy (cryo-EM) and electron cryo-tomography (cryo-ET).
  • Structural modeling and quaternary structure analysis.

Main Results:

  • XL-MS combined with structural modeling has revealed the quaternary structure of interspecies protein complexes.
  • Electron cryo-tomography has visualized bacterial-human interactions during infection.
  • These integrated approaches provide detailed insights into host-pathogen protein complex structures and functions.

Conclusions:

  • AP-MS, XL-MS, cryo-EM, and cryo-ET, coupled with structural modeling, are powerful tools for studying host-pathogen interactions.
  • Future research using these methods will expand knowledge of interaction function, dynamics, and evolution.
  • This enhanced understanding is vital for developing novel drugs and vaccines against infectious diseases.