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Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis

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Collagen-like proteins in pathogenic E. coli strains.

Neelanjana Ghosh¹, Thomas J McKillop, Thomas A Jowitt

¹Manchester Interdisciplinary Biocentre, University of Manchester, Manchester, United Kingdom.

|June 16, 2012

Summary

Enterohaemorrhagic E. coli O157:H7 contains unique collagen-like proteins within prophages that enhance virulence. These proteins, structurally similar to vertebrate collagens, may aid in horizontal gene transfer and bacterial infection.

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Area of Science:

Microbiology
Structural Biology
Genomics

Background:

Enterohaemorrhagic Escherichia coli O157:H7 possesses unique genetic elements not found in laboratory strains.
Prophages within O157:H7 genomes contain genes associated with virulence and horizontal gene transfer.

Purpose of the Study:

To investigate the structure and function of collagen-like proteins encoded by prophages in E. coli O157:H7.
To determine the biophysical properties and potential role of these novel collagen-like molecules.

Main Methods:

Cloning of E. coli O157:H7 collagen-like proteins into a laboratory strain.
Spectroscopic, biophysical, and electron microscopy analyses of recombinant proteins and domains.
Structural characterization including trimer formation and triple helix analysis.

Main Results:

E. coli O157:H7 collagen-like proteins form trimers and possess a collagen triple helical domain.
These proteins exhibit high thermal stability and a unique dumbbell-shaped morphology.
The structure suggests a role as phage tail proteins involved in bacterial attachment.

Conclusions:

Collagen-like proteins in E. coli O157:H7 are structurally analogous to vertebrate collagens but possess distinct features.
Their morphology and stability suggest a function in bacteriophage-mediated virulence gene dissemination.
These findings provide insight into the mechanisms of virulence factor spread in pathogenic bacteria.