Phenotypic characterization of OmpX, an Ail homologue of Yersinia pestis KIM
Abstract
The goal of this study was to characterize the Yersinia pestis KIM OmpX protein. Yersinia spp. provide a model for studying several virulence processes including attachment to, and internalization by, host cells. For Yersinia enterocolitica and Yersinia pseudotuberculosis, Ail, YadA and Inv, have been implicated in these processes. In Y. pestis, YadA and Inv are inactivated. Genomic analysis of two Y. pestis strains revealed four loci with sequence homology to Ail. One of these genes, designated y1324 in the Y. pestis KIM database, encodes a protein designated OmpX. The mature protein has a predicted molecular mass of 17.47 kDa, shares approximately 70 % sequence identity with Y. enterocolitica Ail, and has an identical homologue, designated Ail, in the Y. pestis CO92 database. The present study compared the Y. pestis KIM6(+) parental strain with a mutant derivative having an engineered disruption of the OmpX structural gene. The parental strain (and a merodiploid control strain) expressed OmpX at 28 and 37 degrees C, and the protein was detectable throughout all phases of growth. OmpX was required for efficient adherence to, and internalization by, cultured HEp-2 cell monolayers and conferred resistance to the bactericidal effect of human serum. Deletion of ompX resulted in a significantly reduced autoaggregation phenotype and loss of pellicle formation in vitro. These results suggest that Y. pestis OmpX shares functional homology with Y. enterocolitica Ail in adherence, internalization into epithelial cells and serum resistance.
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Ail is involved in adherence and internalization into epithelial host cells and mediates autoaggregation in Y. pestis.
“Ail is involved in adherence and internalization into epithelial host cells and also mediates autoaggregation in Y. pestis [56].”
From Bacterial autoaggregation (2018) · cites this paper as [56]
Ail-mediated autoaggregation was observed at both 28 °C and 37 °C, but resulting flocs were larger at 28 °C.
“Ail-mediated autoaggregation was observed at both 28 °C and 37 °C, but the resulting flocs were larger at 28 °C.”
From Bacterial autoaggregation (2018) · cites this paper as [56]
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References 65 · Cited by 107
- Authors
- Kolodziejek, A. M., Sinclair, D. J., Seo, K. S., Schnider, D. R., Deobald, C. F., Rohde, H. N., Viall, A. K., Minnich, S. S., Hovde, C. J., Minnich, S. A., & Bohach, G. A.
- Affiliations
- University of Idaho (US)
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 2007-09-01
- Volume
- 153
- Issue
- 9
- Pages
- 2941-2951
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- OpenAlex
- W2141261615
- Cited by
- 107
- References
- 65
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2 · 2023: 3 · 2022: 6 · 2021: 3 · 2020: 7 · 2019: 1 · 2018: 7 · 2017: 4 · 2016: 4 · 2015: 8 · 2014: 6 · 2013: 9 · 2012: 8
- FWCI
- 5.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (U54AI057141, U54-AI57141)
- National Center for Research Resources (P20 RR 15587, P20RR015587, P20RR016454)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Yersinia bacterium, plague, ectoparasites research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
- Keywords
- OmpX, Yersinia pestis, Yersinia enterocolitica, bacterial adhesion, host cell internalization, serum resistance, self-aggregation, pellicle formation, virulence factors, Yersinia pseudotuberculosis
- MeSH terms
- Amino Acid Sequence, Bacterial Adhesion, Bacterial Outer Membrane Proteins, Blood Bactericidal Activity, Cell Line, Epithelial Cells, Humans, Hydrolases, Molecular Sequence Data, Phenotype, Yersinia pestis, Gene Deletion, Sequence Homology, Amino Acid, Computational Biology, Proteome
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