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Cited by 13Escherichia coli research studiesBiochemical and Structural CharacterizationBacterial Genetics and Biotechnology

Self-association motifs in the enteroaggregative Escherichia coli heat-resistant agglutinin 1

Glaubman, Jessica, Hofmann, Jennifer, Bonney, Megan E., Park, Sumin, Thomas, Jessica M., Kokona, Bashkim, Ramos Falcón, Laura I., Chung, Yoonjie K. +2 more·2016·Microbiology
DOI 10.1099/mic.0.000303
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Abstract

The heat-resistant agglutinin 1 (Hra1) is an integral outer membrane protein found in strains of Escherichia coli that are exceptional colonizers. Hra1 from enteroaggregative E. coli strain 042 is sufficient to confer adherence to human epithelial cells and to cause bacterial autoaggregation. Hra1 is closely related to the Tia invasin, which also confers adherence, but not autoaggregation. Here, we have demonstrated that Hra1 mediates autoaggregation by self-association and we hypothesize that at least some surface-exposed amino acid sequences that are present in Hra1, but absent in Tia, represent autoaggregation motifs. We inserted FLAG tags along the length of Hra1 and used immune-dot blots to verify that four in silico-predicted outer loops were indeed surface exposed. In Hra1 we swapped nine candidate motifs in three of these loops, ranging from one to ten amino acids in length, to the corresponding sequences in Tia. Three of the motifs were required for Hra1-mediated autoaggregation. The database was searched for other surface proteins containing these motifs; the GGXWRDDXK motif was also present in a surface-exposed region of Rck, a Salmonella enterica serotype Typhimurium complement resistance protein. Cloning and site-specific mutagenesis demonstrated that Rck can confer weak, GGXWRDDXK-dependent autoaggregation by self-association. Hra1 and Rck appear to form heterologous associations and GGXWRDDXK is required on both molecules for Hra1-Rck association. However, a GGYWRDDLKE peptide was not sufficient to interfere with Hra1-mediated autoaggregation. In the present study, three autoaggregation motifs in an integral outer membrane protein have been identified and it was demonstrated that at least one of them works in the context of a different cell surface.

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  • Self-association motifs or residues have been found in some proteins, such as the outer membrane proteins Hek from E. coli and Ail from Y. pestis.

    “Self-association motifs or residues have been found in some proteins, such as the outer membrane proteins Hek from E. coli [65] and Ail from Y. pestis [83].”

    From Bacterial autoaggregation (2018) · cites this paper as [65]

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  • Bacterial autoaggregation

    Trunk, T., Bacterial Cell Surface Group, S. F. G. A. E. B., S. Khalil, H., & C. Leo, J. (2018) · AIMS Microbiology · doi:10.3934/microbiol.2018.1.140 · Cited by 444 · see citing works

    “These proteins consist of a β-barrel transmembrane domain, the loops of which extend into the extracellular space and can thus interact with loops from proteins on the surface of a neighbouring bacterium [65].”
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Related

Authors
Glaubman, J., Hofmann, J., Bonney, M. E., Park, S., Thomas, J. M., Kokona, B., Ramos Falcón, L. I., Chung, Y. K., Fairman, R., & Okeke, I. N.
Affiliations
  • Haverford College (US)
  • Department of Biology, Haverford College, Haverford, PA, USA
ORCID
Venue
Microbiology
Publisher
Microbiology Society
Published
2016-07-01
Volume
162
Issue
7
Pages
1091-1102
ISSN
  • 1350-0872 (ISSN-L)
  • 1465-2080
DOI
10.1099/mic.0.000303
OpenAlex
W2386617778
Cited by
13
References
45
Citations by year
2026: 1 · 2024: 1 · 2022: 3 · 2021: 3 · 2020: 2 · 2018: 2 · 2017: 1
FWCI
0.96
Type
journal article
Language
en
Open access
closed
Locations
  • Microbiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
Howard Hughes Medical Institute
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
enteroaggregative Escherichia coli, self-aggregation, outer membrane proteins, surface-exposed loops, bacterial adhesion, site-directed mutagenesis
MeSH terms
Amino Acid Sequence, Bacterial Adhesion, Bacterial Outer Membrane Proteins, Base Sequence, Escherichia coli, Salmonella typhimurium, Mutagenesis, Site-Directed, Sequence Alignment, Sequence Analysis, DNA, Adhesins, Bacterial, Amino Acid Motifs, Escherichia coli Proteins

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