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

Complement System01:27

Complement System

12.3K
The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
12.3K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

4.4K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
4.4K
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

922
Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
922
Antibody Actions01:26

Antibody Actions

3.5K
Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
3.5K
Protein Complex Assembly02:41

Protein Complex Assembly

17.1K
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...
17.1K
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

4.5K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
4.5K

You might also read

Related Articles

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

Sort by
Same author

Dysregulation of complement at the synapse in P301S mice and human tauopathies.

Acta neuropathologica communications·2026
Same author

Advances in cryo-EM that have shaped mechanistic models of membrane-attack-complex assembly and regulation.

IUCrJ·2026
Same author

Structural basis of human γTuRC closure during CM1-activated microtubule nucleation.

Nature communications·2026
Same author

Structural basis for Rep-mediated adeno-associated virus packaging.

Cell reports·2026
Same author

Activation of the Lectin Pathway Drives Persistent Complement Dysregulation in Long COVID.

Immunology·2026
Same author

Absence of complement terminal pathway activity in C6-deficient mice prolongs survival in a mouse model of severe malarial infection.

Immunobiology·2025
Same journal

Kat5 deficiency in alveolar type II cells licenses STAT6-driven glycolytic reprogramming and pulmonary fibrosis.

Nature communications·2026
Same journal

Continuous nonthermal slab gap formed by progressive tearing beneath Northeast Asia.

Nature communications·2026
Same journal

Zeolitic isolated protonic acid sites-mediated NH<sub>3</sub> storage for robust NO<sub>x</sub> removal.

Nature communications·2026
Same journal

Coaxially nested component with asymmetric fiber resonant cavity and separation membrane for gaseous and dissolved gases detection.

Nature communications·2026
Same journal

Near-unity charge readout signal in a nonlinear resonator without matching the sensor dissipation.

Nature communications·2026
Same journal

Prokaryotic Schlafen proteins cleave tRNAs during type III CRISPR immunity.

Nature communications·2026
See all related articles

Related Experiment Video

Updated: Mar 26, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

12.3K

Structural basis of complement membrane attack complex formation.

Marina Serna1, Joanna L Giles2, B Paul Morgan2

  • 1Department of Life Sciences, Imperial College London, Sir Ernst Chain Building, South Kensington Campus, London SW7 2AZ, UK.

Nature Communications
|February 5, 2016
PubMed
Summary
This summary is machine-generated.

The membrane attack complex (MAC) forms pores in cell membranes. This study reveals the human MAC structure, showing a unique split-washer shape and irregular pore formation mechanism.

More Related Videos

Measuring the 50% Haemolytic Complement CH50 Activity of Serum
08:26

Measuring the 50% Haemolytic Complement CH50 Activity of Serum

Published on: March 29, 2010

39.1K
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

10.0K

Related Experiment Videos

Last Updated: Mar 26, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

12.3K
Measuring the 50% Haemolytic Complement CH50 Activity of Serum
08:26

Measuring the 50% Haemolytic Complement CH50 Activity of Serum

Published on: March 29, 2010

39.1K
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

10.0K

Area of Science:

  • Structural Biology
  • Immunology
  • Molecular Biology

Background:

  • The membrane attack complex (MAC) is crucial for complement-mediated lysis of pathogens.
  • Sublytic MAC pores on host cells can trigger signaling pathways.
  • Previous structural data on MAC components and assembly mechanisms were incomplete.

Purpose of the Study:

  • To determine the high-resolution structure of the human MAC.
  • To elucidate the molecular details of MAC assembly and its mechanism of pore formation.

Main Methods:

  • Electron cryo-microscopy (cryo-EM) was used to determine the structure of human MAC.
  • Subnanometer resolution structural analysis was performed.

Main Results:

  • The complete human MAC structure was resolved at subnanometer resolution.
  • MAC adopts a distinct 'split-washer' configuration, differing from other pore-forming proteins.
  • Assembly involves precursors partially penetrating the lipid bilayer, forming an irregular β-barrel pore.

Conclusions:

  • The study defines the stoichiometry and interaction interfaces governing MAC assembly.
  • The unique structure explains the molecular basis of MAC pore formation.
  • A novel mechanism of action for MAC is proposed, extending beyond simple membrane penetration.