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Collagen-Like Proteins in Pathogenic E. coli Strains

The genome sequences of enterohaemorrhagic E. coli O157:H7 strains show multiple open-reading frames with collagen-like sequences that are absent from the common laboratory strain K-12. These putative collagens are included in prophages embedded in O157:H7 genomes. These prophages carry numerous gen...

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Autores principales: Ghosh, Neelanjana, McKillop, Thomas J., Jowitt, Thomas A., Howard, Marjorie, Davies, Heather, Holmes, David F., Roberts, Ian S., Bella, Jordi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3368898/
https://www.ncbi.nlm.nih.gov/pubmed/22701585
http://dx.doi.org/10.1371/journal.pone.0037872
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author Ghosh, Neelanjana
McKillop, Thomas J.
Jowitt, Thomas A.
Howard, Marjorie
Davies, Heather
Holmes, David F.
Roberts, Ian S.
Bella, Jordi
author_facet Ghosh, Neelanjana
McKillop, Thomas J.
Jowitt, Thomas A.
Howard, Marjorie
Davies, Heather
Holmes, David F.
Roberts, Ian S.
Bella, Jordi
author_sort Ghosh, Neelanjana
collection PubMed
description The genome sequences of enterohaemorrhagic E. coli O157:H7 strains show multiple open-reading frames with collagen-like sequences that are absent from the common laboratory strain K-12. These putative collagens are included in prophages embedded in O157:H7 genomes. These prophages carry numerous genes related to strain virulence and have been shown to be inducible and capable of disseminating virulence factors by horizontal gene transfer. We have cloned two collagen-like proteins from E. coli O157:H7 into a laboratory strain and analysed the structure and conformation of the recombinant proteins and several of their constituting domains by a variety of spectroscopic, biophysical, and electron microscopy techniques. We show that these molecules exhibit many of the characteristics of vertebrate collagens, including trimer formation and the presence of a collagen triple helical domain. They also contain a C-terminal trimerization domain, and a trimeric α-helical coiled-coil domain with an unusual amino acid sequence almost completely lacking leucine, valine or isoleucine residues. Intriguingly, these molecules show high thermal stability, with the collagen domain being more stable than those of vertebrate fibrillar collagens, which are much longer and post-translationally modified. Under the electron microscope, collagen-like proteins from E. coli O157:H7 show a dumbbell shape, with two globular domains joined by a hinged stalk. This morphology is consistent with their likely role as trimeric phage side-tail proteins that participate in the attachment of phage particles to E. coli target cells, either directly or through assembly with other phage tail proteins. Thus, collagen-like proteins in enterohaemorrhagic E. coli genomes may have a direct role in the dissemination of virulence-related genes through infection of harmless strains by induced bacteriophages.
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spelling pubmed-33688982012-06-13 Collagen-Like Proteins in Pathogenic E. coli Strains Ghosh, Neelanjana McKillop, Thomas J. Jowitt, Thomas A. Howard, Marjorie Davies, Heather Holmes, David F. Roberts, Ian S. Bella, Jordi PLoS One Research Article The genome sequences of enterohaemorrhagic E. coli O157:H7 strains show multiple open-reading frames with collagen-like sequences that are absent from the common laboratory strain K-12. These putative collagens are included in prophages embedded in O157:H7 genomes. These prophages carry numerous genes related to strain virulence and have been shown to be inducible and capable of disseminating virulence factors by horizontal gene transfer. We have cloned two collagen-like proteins from E. coli O157:H7 into a laboratory strain and analysed the structure and conformation of the recombinant proteins and several of their constituting domains by a variety of spectroscopic, biophysical, and electron microscopy techniques. We show that these molecules exhibit many of the characteristics of vertebrate collagens, including trimer formation and the presence of a collagen triple helical domain. They also contain a C-terminal trimerization domain, and a trimeric α-helical coiled-coil domain with an unusual amino acid sequence almost completely lacking leucine, valine or isoleucine residues. Intriguingly, these molecules show high thermal stability, with the collagen domain being more stable than those of vertebrate fibrillar collagens, which are much longer and post-translationally modified. Under the electron microscope, collagen-like proteins from E. coli O157:H7 show a dumbbell shape, with two globular domains joined by a hinged stalk. This morphology is consistent with their likely role as trimeric phage side-tail proteins that participate in the attachment of phage particles to E. coli target cells, either directly or through assembly with other phage tail proteins. Thus, collagen-like proteins in enterohaemorrhagic E. coli genomes may have a direct role in the dissemination of virulence-related genes through infection of harmless strains by induced bacteriophages. Public Library of Science 2012-06-06 /pmc/articles/PMC3368898/ /pubmed/22701585 http://dx.doi.org/10.1371/journal.pone.0037872 Text en Ghosh et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Ghosh, Neelanjana
McKillop, Thomas J.
Jowitt, Thomas A.
Howard, Marjorie
Davies, Heather
Holmes, David F.
Roberts, Ian S.
Bella, Jordi
Collagen-Like Proteins in Pathogenic E. coli Strains
title Collagen-Like Proteins in Pathogenic E. coli Strains
title_full Collagen-Like Proteins in Pathogenic E. coli Strains
title_fullStr Collagen-Like Proteins in Pathogenic E. coli Strains
title_full_unstemmed Collagen-Like Proteins in Pathogenic E. coli Strains
title_short Collagen-Like Proteins in Pathogenic E. coli Strains
title_sort collagen-like proteins in pathogenic e. coli strains
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3368898/
https://www.ncbi.nlm.nih.gov/pubmed/22701585
http://dx.doi.org/10.1371/journal.pone.0037872
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