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

Antibody Structure01:10

Antibody Structure

12.0K
12.0K
Antibody Structure01:10

Antibody Structure

51.5K
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...
51.5K
Antibody Structure and Classes01:25

Antibody Structure and Classes

7.6K
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
7.6K
Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

14.0K
In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or...
14.0K
Cytomegalovirus Disease01:27

Cytomegalovirus Disease

92
Cytomegalovirus (CMV) disease is caused by human cytomegalovirus, a double-stranded DNA virus of the Herpesviridae family. While primary CMV infection is often asymptomatic in immunocompetent individuals, the virus can cause severe disease in neonates and immunocompromised patients. CMV is the most common cause of congenital viral infection in the United States, and a major pathogen in solid organ and hematopoietic stem cell transplant recipients.CMV is transmitted via bodily fluids, sexual...
92
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

3.3K
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...
3.3K

You might also read

Related Articles

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

Sort by
Same author

Comparison of Igκ and Igλ binding toward influenza virus hemagglutinin and SARS-CoV-2 Spike protein during primary viral infections in humans, mice, and pigs.

Comparative immunology, microbiology and infectious diseases·2026
Same author

Congenital central nervous system malformations in piedmontese calves-part 1. structural brain disorders.

Frontiers in veterinary science·2026
Same author

Human broadly neutralizing influenza B virus antibodies recognizing hemagglutinin computationally optimized broadly reactive antigens.

Frontiers in immunology·2026
Same author

ReVesicle: Curation and Equilibration of Lipid Vesicles for Mesoscale Simulations.

Journal of chemical theory and computation·2026
Same author

Delineation of the antibody light chain biases and kinetics following primary and secondary influenza virus infections of ferrets.

ImmunoHorizons·2026
Same author

Extended Heterosubtypic Neutralization and Preclinical Model In Vivo Protection from Clade 2.3.4.4b H5 Influenza Virus Infection by Broadly Neutralizing Antibodies.

Vaccines·2026

Related Experiment Video

Updated: Apr 25, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
07:10

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Published on: September 14, 2014

13.8K

HCV E2 core structures and mAbs: something is still missing.

Matteo Castelli1, Nicola Clementi1, Giuseppe A Sautto1

  • 1Laboratory of Microbiology and Virology, Università "Vita-Salute" San Raffaele, Milano, Italy.

Drug Discovery Today
|August 31, 2014
PubMed
Summary
This summary is machine-generated.

Developing effective hepatitis C virus (HCV) vaccines is hindered by unknown E2 surface protein structures. This study proposes a new structural model for E2 glycoprotein, crucial for HCV entry, reconciling existing data and antibody reactivity.

More Related Videos

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors
16:49

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Published on: July 16, 2012

11.2K
Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.2K

Related Experiment Videos

Last Updated: Apr 25, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
07:10

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

Published on: September 14, 2014

13.8K
Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors
16:49

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Published on: July 16, 2012

11.2K
Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.2K

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Hepatitis C virus (HCV) vaccine development is limited by a lack of structural data for its surface proteins.
  • The E2 surface glycoprotein is key for HCV entry, but its overall structure remains elusive.
  • Existing crystallographic data of the E2 core (E2c) conflict with biochemical and functional studies.

Purpose of the Study:

  • To address the discrepancies in structural and functional data of the HCV E2 glycoprotein.
  • To propose an alternative disulfide bridge pattern for E2 based on antibody reactivity.
  • To develop a computational model of E2 that aligns with all available experimental evidence.

Main Methods:

  • Literature review of existing structural and functional studies on HCV E2.
  • Analysis of unpublished human monoclonal antibody reactivity data.
  • Development of a protein modeling strategy for the E2 glycoprotein.

Main Results:

  • Identified significant disagreements between E2c structures and biochemical/functional data.
  • Proposed a novel disulfide bridge pattern for E2.
  • Initiated a modeling approach to integrate diverse E2 data.

Conclusions:

  • The current understanding of E2 structure is incomplete and potentially inaccurate.
  • A revised structural model, incorporating antibody data, is necessary for understanding HCV entry.
  • Further structural and modeling studies are crucial for advancing HCV vaccine design.