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

You might also read

Related Articles

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

Sort by
Same author

Total Synthesis of Conjugation-Ready Sulfated Red Algae Carrageenan Oligosaccharides for Sensing Applications.

Journal of the American Chemical Society·2026
Same author

Correction to "Pairing Nanoparticles Geometry with TLR Agonists to Modulate Immune Responses for Vaccine Development".

ACS applied bio materials·2026
Same author

Correction to "The Shape of Nanostructures Encodes Immunomodulation of Carbohydrate Antigen and Vaccine Development".

ACS chemical biology·2026
Same author

Human-specific evolutionary genetic loss of addition of a single oxygen atom from sialic acids increases hydrophobicity of cells and proteins [Carbohydr. Res. (552), June 2025, 109469].

Carbohydrate research·2026
Same author

Correction to "Imaging and Targeting of the α(2-6) and α(2-3) Linked Sialic Acid Quantum Dots in Zebrafish and Mouse Models".

ACS applied materials & interfaces·2026
Same author

Expeditious synthesis of multiglycopeptides with heterogeneous glycan cores derived from an α-dystroglycan mucin-like domain.

Organic & biomolecular chemistry·2026

Related Experiment Video

Updated: Jun 11, 2025

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

12.7K

Impedimetric Characterization of NanA Structural Domains Activity on Sialoside-Containing Interfaces.

Israel Alshanski1, Suraj Toraskar2, Karin Mor1

  • 1The Institute of Chemistry and Center of Nanotechnology, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.

Langmuir : the ACS Journal of Surfaces and Colloids
|October 8, 2024
PubMed
Summary

Researchers studied the neuraminidase NanA from Streptococcus pneumoniae, separating its two domains. They found each domain has unique sialoside binding and catalytic preferences, offering insights into enzyme function.

More Related Videos

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
08:16

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

389
Detection of Neu1 Sialidase Activity in Regulating TOLL-like Receptor Activation
09:04

Detection of Neu1 Sialidase Activity in Regulating TOLL-like Receptor Activation

Published on: September 7, 2010

11.5K

Related Experiment Videos

Last Updated: Jun 11, 2025

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

12.7K
Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
08:16

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

389
Detection of Neu1 Sialidase Activity in Regulating TOLL-like Receptor Activation
09:04

Detection of Neu1 Sialidase Activity in Regulating TOLL-like Receptor Activation

Published on: September 7, 2010

11.5K

Area of Science:

  • Biochemistry
  • Microbiology
  • Surface Science

Background:

  • Streptococcus pneumoniae possesses surface-bound neuraminidase NanA, crucial for pathogenesis.
  • NanA has two domains that interact with sialosides, but their individual contributions are difficult to isolate.

Purpose of the Study:

  • To biochemically separate NanA domains and analyze their distinct binding and catalytic properties.
  • To investigate domain-specific interactions with surface-bound sialosides using electrochemical methods.

Main Methods:

  • Biochemical separation of NanA domains.
  • Electrochemical techniques including impedance spectroscopy.
  • Surface analysis on varied surfaces with sialoside libraries.

Main Results:

  • Each NanA domain exhibits specific sialoside affinity and preferences.
  • Protein-surface interactions using impedance revealed unique domain contributions.
  • The carbohydrate-binding domain increases impedance and binds to sialoside surfaces.
  • The catalytic domain binds surfaces at high concentrations but retains activity at low concentrations.

Conclusions:

  • Separated NanA domains possess distinct functional characteristics.
  • Electrochemical surface analysis is a valuable tool for probing enzyme domain contributions.
  • Understanding domain-specific interactions is key to elucidating NanA's role in pneumococcal pathogenesis.