Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Fimbriae, Pili, and Axial Filaments

Fimbriae, Pili, and Axial Filaments

Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...

Mechanism of Filopodia Formation

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...

Globular and Fibrous Proteins

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

Protein-protein Interfaces

Protein-protein Interfaces

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 polypeptide...

Surface Appendages of Archaea

Surface Appendages of Archaea

Archaeal surface appendages are highly specialized structures essential for environmental adaptation, encompassing roles in adhesion, biofilm formation, and motility. Among these appendages, pili and archaella stand out for their distinct morphologies and functionalities, enabling archaea to thrive in diverse and often extreme environments.Pili: Adhesion and Biofilm FormationPili are filamentous structures assembled from pilin protein subunits, primarily contributing to adhesion and biofilm...

You might also read

Related Articles

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

Sort by

Same author

Targeting the Akt-EphA2 axis and cell-cell adhesion enhances anoikis sensitivity in cancer cells.

Scientific reports·2026

Same author

Low-frequency ultrasound treatment reduces susceptibility to <i>Salmonella</i> infection in aged mice.

Journal of bacteriology·2025

Same author

Low-frequency ultrasound reverses insulin resistance and diabetes-induced changes in the muscle transcriptome in aged mice.

American journal of physiology. Endocrinology and metabolism·2025

Same author

Rejuvenation of Senescent Cells, In Vitro and In Vivo, by Low-Frequency Ultrasound.

Aging cell·2025

Same author

Statistical Mechanics Approach to DNA-Driven Droplet Deformation and Adhesion.

Physical review letters·2025

Same author

Evolving Motility of Active Droplets Is Captured by a Self-Repelling Random Walk Model.

Physical review letters·2025

Search research articles

Related Experiment Video

Updated: Jun 12, 2026

DNA Tension Probes to Map the Transient Piconewton Receptor Forces by Immune Cells

DNA Tension Probes to Map the Transient Piconewton Receptor Forces by Immune Cells

Published on: March 20, 2021

Force-dependent polymorphism in type IV pili reveals hidden epitopes.

Nicolas Biais¹, Dustin L Higashi, Jasna Brujic

¹Department of Biological Sciences, Columbia University, 1212 Amsterdam Avenue, New York, NY 10027, USA. nb2200@columbia.edu

Proceedings of the National Academy of Sciences of the United States of America

|June 11, 2010

Summary

Nature

More Related Videos

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

Related Experiment Videos

Last Updated: Jun 12, 2026

DNA Tension Probes to Map the Transient Piconewton Receptor Forces by Immune Cells

DNA Tension Probes to Map the Transient Piconewton Receptor Forces by Immune Cells

Published on: March 20, 2021

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

Area of Science:

Bacteriology
Structural Biology
Biophysics

Background:

Type IV pili (Tfp) are essential nanometric structures in bacteria, including pathogens like Neisseria gonorrhoeae.
The diverse functions of Tfp are not fully explained by their known structure.
Understanding Tfp dynamics is crucial for explaining bacterial pathogenesis and host interaction.

Purpose of the Study:

To investigate the structural changes in Neisseria gonorrhoeae Type IV pili under applied force.
To uncover novel force-induced conformations of Tfp and their functional implications.
To explore the potential for structural plasticity in biological polymers.

Main Methods:

Utilized optical tweezers, magnetic tweezers, atomic force microscopy, and molecular combing.
Applied controlled forces (approx. 100 pN) to purified Tfp.
Analyzed structural transitions and epitope exposure using biophysical techniques.

Main Results:

Discovered a reversible, force-induced quaternary structure in N. gonorrhoeae Tfp.
Tfp elongated approximately 3-fold and narrowed by 40% under force, returning to original state upon release.
Force-induced conformation exposed previously buried epitopes on the Tfp fiber.

Conclusions:

The force-induced conformational change allows N. gonorrhoeae to maintain host attachment under environmental stress.
This structural plasticity offers a mechanism for bacterial survival and interaction.
Findings necessitate a re-evaluation of Tfp functions and the structural diversity of helical polymers.