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Related Experiment Video

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Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay

Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay

Published on: July 13, 2017

Microbial recognition of human cell surface glycoconjugates.

Anne Imberty¹, Annabelle Varrot

¹CERMAV-CNRS (UPR5301, affiliated with Université Joseph Fourier and belonging to ICMG), BP53, F38041 Grenoble Cedex 9, France. imberty@cermav.cnrs.fr

Current Opinion in Structural Biology

|September 24, 2008

Summary

Pathogens infect hosts by binding to cell surfaces using sugar-binding proteins like lectins. Understanding these interactions reveals specific binding modes crucial for infection strategies.

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Area of Science:

Microbiology
Structural Biology
Glycobiology

Background:

Pathogen infection initiates with host cell surface recognition and adhesion.
Microorganisms utilize lectins and adhesins to bind host glycoconjugates, targeting sialylated and fucosylated oligosaccharides.

Purpose of the Study:

To investigate the molecular mechanisms of pathogen adhesion to host cells.
To elucidate the structural basis of lectin-glycoconjugate interactions in host-pathogen systems.

Main Methods:

Analysis of crystal structures of pathogen receptors bound to host glycans.
Comparative structural analysis of viral, bacterial, and parasite receptors.

Main Results:

Revealed novel protein folds and sugar-binding modes in pathogen receptors.
Demonstrated high specificity in lectin/glycoconjugate interactions, often involving multivalency for enhanced binding affinity.
Highlighted the precise correlation between host tissue glycosylation patterns and specific lectin recognition.

Conclusions:

Structural insights into lectin-glycoconjugate interactions provide a deeper understanding of pathogen invasion mechanisms.
The specificity of these interactions is critical for host-pathogen recognition and subsequent infection.
This knowledge can inform the development of novel anti-infective strategies targeting pathogen adhesion.