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

2.3K
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...
2.3K
Conjugated Proteins02:50

Conjugated Proteins

18.3K
Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
18.3K
Leaky Scanning02:28

Leaky Scanning

5.1K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.1K
Antigen Processing Pathways01:31

Antigen Processing Pathways

989
MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...
989

You might also read

Related Articles

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

Sort by
Same author

Molecular Views into the Synthesis and Activation of Flavocytochrome <i>b</i><sub>558</sub> in Phagocytic Cells-Focus on the Role of EROS.

Antioxidants (Basel, Switzerland)·2026
Same author

Exome sequencing enables molecular diagnosis in 10% of early-onset or familial systemic lupus erythematosus cases.

EBioMedicine·2026
Same author

Enhancing lectin recognition via precise fluorination: Man<sub>5</sub> glycomimetics for targeting DC-SIGN.

Bioorganic chemistry·2026
Same author

Neutralizing human monoclonal antibodies that target the PcrV component of the type III secretion system of <i>Pseudomonas aeruginosa</i> act through distinct mechanisms.

eLife·2026
Same author

Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.

Angewandte Chemie (International ed. in English)·2025
Same author

Efficacy, safety, pharmacokinetics, immunogenicity, and serum neutralizing activity of AZD7442 (tixagevimab-cilgavimab) in patients hospitalized with COVID-19: long-term results from the DisCoVeRy trial.

Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases·2025

Related Experiment Video

Updated: Jun 23, 2025

Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques
08:07

Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques

Published on: January 12, 2024

699

Revisiting the interaction between complement lectin pathway protease MASP-2 and SARS-CoV-2 nucleoprotein.

Isabelle Bally1, Guillaume Drumont1, Véronique Rossi1

  • 1Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.

Frontiers in Immunology
|June 24, 2024
PubMed
Summary
This summary is machine-generated.

The SARS-CoV-2 nucleoprotein does not activate the lectin complement pathway. However, it binds to MASP-2 and undergoes proteolysis, a finding needing further study for its role in COVID-19.

Keywords:
MASP-2SARS-CoV-2complement systemlectin pathwaynucleoprotein

More Related Videos

Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.3K
A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
07:53

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

Published on: January 9, 2019

33.2K

Related Experiment Videos

Last Updated: Jun 23, 2025

Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques
08:07

Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques

Published on: January 12, 2024

699
Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.3K
A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
07:53

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

Published on: January 9, 2019

33.2K

Area of Science:

  • Immunology
  • Virology
  • Biochemistry

Background:

  • Complement activation contributes to severe SARS-CoV-2 pathogenesis via inflammatory responses.
  • The lectin complement pathway, initiated by mannose-binding lectin (MBL) recognizing the Spike glycoprotein, is crucial for innate antiviral defense.
  • Previous studies suggested SARS-CoV-2 nucleoprotein (N) interaction with MASP-2 potentiates the lectin pathway.

Purpose of the Study:

  • To re-investigate the interaction between SARS-CoV-2 nucleoprotein (N) and mannose-binding lectin-associated serine protease 2 (MASP-2).
  • To clarify the role of N protein in MBL-mediated lectin pathway activation.
  • To explore potential functional significance of N protein and MASP-2 interaction in SARS-CoV-2 infection.

Main Methods:

  • Investigated interactions between SARS-CoV-2 N protein (bacterial or mammalian origin) and full-length or catalytic domain of MASP-2 (active or proenzyme forms).
  • Assessed N protein binding to MASP-2 and its role in MBL-mediated lectin pathway activation.
  • Analyzed proteolysis of N protein upon incubation with MASP-2.

Main Results:

  • Confirmed N protein binding to proenzyme MASP-2 but not to the MASP-2 catalytic domain.
  • Found no evidence for N protein involvement in MBL-mediated lectin pathway activation.
  • Observed proteolysis of the SARS-CoV-2 N protein when incubated with MASP-2.

Conclusions:

  • The SARS-CoV-2 nucleoprotein does not appear to potentiate MBL-initiated lectin pathway activation.
  • N protein interacts with proenzyme MASP-2, leading to its own proteolysis.
  • The functional significance of N protein proteolysis by MASP-2 in SARS-CoV-2 infected patients requires further investigation.