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Related Experiment Video

Updated: Jun 4, 2026

A Novel Method for Assessing Proximal and Distal Forelimb Function in the Rat: the Irvine, Beatties and Bresnahan (IBB) Forelimb Scale

A Novel Method for Assessing Proximal and Distal Forelimb Function in the Rat: the Irvine, Beatties and Bresnahan (IBB) Forelimb Scale

Published on: December 16, 2010

Fold and function of the InlB B-repeat.

Maria Ebbes¹, Willem M Bleymüller, Mihaela Cernescu

¹Department of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.

The Journal of Biological Chemistry

|February 25, 2011

Summary

The Listeria monocytogenes invasion protein InlB

Area of Science:

Microbiology
Structural Biology
Cell Biology

Background:

Listeria monocytogenes invasion relies on the InlB protein, which binds host cell receptor tyrosine kinase Met.
InlB's N-terminal internalin domain binds Met, while C-terminal GW domains bind glycosaminoglycans (GAGs).
The function of InlB's central B-repeat region remains largely uncharacterized.

Purpose of the Study:

To structurally and functionally characterize the InlB B-repeat domain.
To investigate the B-repeat's role in Listeria monocytogenes host cell invasion and motility.

Main Methods:

X-ray crystallography to determine the B-repeat structure.
Cellular assays to assess the B-repeat's functional contribution to invasion and motility.

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Bimolecular Fluorescence Complementation

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

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Last Updated: Jun 4, 2026

A Novel Method for Assessing Proximal and Distal Forelimb Function in the Rat: the Irvine, Beatties and Bresnahan (IBB) Forelimb Scale

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Published on: December 16, 2010

Application of Biolayer Interferometry (BLI) for Studying Protein-Protein Interactions in Transcription

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Bimolecular Fluorescence Complementation

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Main Results:

The InlB B-repeat adopts a novel β-grasp fold, structurally similar to SUMOs and bacterial mucin-binding proteins.
This B-repeat represents a new domain family found in numerous bacterial proteins, likely acting as a spacer or receptor-binding domain.
The B-repeat enhances InlB's ability to stimulate cell motility, acting synergistically with the internalin domain.

Conclusions:

The InlB B-repeat likely binds an additional host cell receptor, augmenting Met signaling and enhancing Listeria monocytogenes invasion.
This study reveals a novel domain structure and function, expanding our understanding of bacterial invasion mechanisms.