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

11.8K
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...
11.8K
Antimicrobial Proteins01:23

Antimicrobial Proteins

15.2K
Antimicrobial proteins are important components of the immune system. They aid the body in combating pathogens by either killing them directly or hindering their replication processes. Four main types of antimicrobial substances are interferons, the complement system, iron-binding proteins, and antimicrobial proteins.
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
15.2K
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
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.0K
Regulation of Hematopoietic Stem Cells01:01

Regulation of Hematopoietic Stem Cells

4.3K
All blood and immune cells are produced from the multipotent hematopoietic stem cells (HSCs) by the process of hematopoiesis. However, they all have a limited life span. In addition, many are depleted in immune surveillance or combatting an injury or infection. This makes blood one of the most regenerative tissues. Hematopoiesis helps replenish these blood and immune cells, restoring the body's normal functioning. However, overproduction of blood and immune cells can make them cancerous or...
4.3K
Hypersensitivity Reactions: Immune-Complex Reactions01:19

Hypersensitivity Reactions: Immune-Complex Reactions

82
Type III hypersensitivity reactions occur when antigen–antibody complexes form and activate the complement system. Normally, these complexes help the clearance of antigens by phagocytes and red blood cells. However, when large numbers of immune complexes are present, they can deposit in tissues—particularly in the walls of blood vessels—leading to inflammation and tissue injury. These deposits trigger complement activation and neutrophil recruitment, resulting in serum...
82

You might also read

Related Articles

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

Sort by
Same author

COSMIC-Linked Ras Mutations at the Interface Between H-Ras and PI3Kγ<sub>RBD</sub> Frequently Generate Affinity Increases.

Biochemistry·2026
Same author

Sabbatical.

Academic medicine : journal of the Association of American Medical Colleges·2026
Same author

Retinopathy caused by a primary immune regulatory disorder - the spectrum of AIRE-associated retinopathy: case series and literature review.

Eye (London, England)·2026
Same author

Complement biomarkers during iptacopan treatment.

Lancet (London, England)·2026
Same author

C4b-binding protein as an antigenic target in the pathogenesis of antiphosphatidylethanolamine autoantibodies.

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

Carotenoid Status and Psychological Impact of Presymptomatic Macular Degeneration Genetic Risk Assessment: The MAGENTA Randomized Trial.

Ophthalmology science·2026

Related Experiment Video

Updated: Mar 12, 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

Mapping the Complement Factor H-Related Protein 1 (CFHR1):C3b/C3d Interactions.

Jonathan P Hannan1, Jennifer Laskowski1, Joshua M Thurman1

  • 1Department of Medicine, University of Colorado School of Medicine, Aurora, Colorado, United States of America.

Plos One
|November 5, 2016
PubMed
Summary
This summary is machine-generated.

Complement factor H-related protein 1 (CFHR1) regulates complement by binding to C3b and C3d. Dimerized CFHR1 competes with complement factor H (CFH) and CFH-like protein 1 (CFHL-1) for these binding sites.

More Related Videos

Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry
07:20

Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry

Published on: May 19, 2020

7.8K
Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

6.5K

Related Experiment Videos

Last Updated: Mar 12, 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 Erythrocyte Complement Receptor 1 Using Flow Cytometry
07:20

Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry

Published on: May 19, 2020

7.8K
Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

6.5K

Area of Science:

  • Immunology
  • Molecular Biology

Background:

  • Complement factor H-related protein 1 (CFHR1) is a known regulator of the complement system.
  • CFHR1 inhibits complement by blocking C5 convertase activity and interfering with C5b surface binding.
  • CFHR1 antagonizes complement factor H (CFH) regulation on cell surfaces by competing for C3b binding.

Purpose of the Study:

  • To identify the specific binding interface of CFHR1 with complement components C3b and C3d.
  • To determine the role of CFHR1 dimerization in its interaction with C3b/C3d and CFH.
  • To investigate the competitive binding of CFHR1 with CFH and CFH-like protein 1 (CFHL-1).

Main Methods:

  • Site-directed mutagenesis was employed to pinpoint the CFHR1 binding interface.
  • ELISA-based and functional assays were utilized to analyze binding interactions.
  • Competitive binding assays were performed using CFH and CFHL-1.

Main Results:

  • A single, shared interface was identified for CFHR1 binding to C3b and C3d.
  • This interface is identical to the C3b binding site of CFH's C-terminal domains (SCR19-20).
  • CFHR1 dimerization is essential for effective binding to C3b/C3d and competition with CFH.
  • CFHR1 competes with CFHL-1 for C3b binding, blocking both N- and C-terminal CFH interactions with C3b.

Conclusions:

  • CFHR1 binds C3b and C3d via a specific interface involving its C-terminal domains.
  • CFHR1 dimerization is crucial for its regulatory function and competition with CFH.
  • CFHR1 acts as a potent complement regulator by sterically hindering CFH binding to C3b.