ArticleInfection and immunity2010
Functional characterization of the IlpA protein of Vibrio vulnificus as an adhesin and its role in bacterial pathogenesis.
Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
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- Clonal Dynamics, Virulence Genes, Antimicrobial Resistance, and Early Diagnostic Indicators of Bloodstream Infections ofInfection and drug resistance · 2025Article
- Identification and whole-genome sequencing analysis of Vibrio vulnificus strains causing pearl gentian grouper disease in China.BMC microbiology · 2022Article
- Population genomics of the food-borne pathogenMicrobial genomics · 2022Article
- Whole genome sequencing of the multidrug-resistantFrontiers in medicine · 2022Article
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- The antibiotic resistance and pathogenicity of a multidrug-resistant Elizabethkingia anophelis isolate.MicrobiologyOpen · 2019Article
- Role of Heat Shock Proteases in Quorum-Sensing-Mediated Regulation of Biofilm Formation bymBio · 2018Article
- Phylogeny ofFrontiers in microbiology · 2017Article
- Regulatory Characteristics of Vibrio vulnificus gbpA Gene Encoding a Mucin-binding Protein Essential for Pathogenesis.The Journal of biological chemistry · 2016Article
- Vibrio vulnificus VvhA induces NF-κB-dependent mitochondrial cell death via lipid raft-mediated ROS production in intestinal epithelial cells.Cell death & disease · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vibrio vulnificus is a Gram-negative bacterium that causes a fatal septicemia. One of its virulence factors is a membrane-bound lipoprotein, IlpA, which can induce cytokine production in human immune cells. In the present study, the role of IlpA as an adhesion molecule was investigated. An ilpA-deleted V. vulnificus mutant showed significantly decreased adherence to INT-407 human intestinal epithelial cells, which in turn resulted in reduced cytotoxicity. The DeltailpA mutant recovered the adherence ability of the wild type by complementation in trans with the intact ilpA gene. In addition, pretreatment of V. vulnificus with anti-IlpA polyclonal antibodies resulted in a significant reduction of bacterial adherence. To localize the domain of IlpA required for cytoadherence, three truncated recombinant IlpA polypeptides were constructed and tested for the ability to adhere to human cells by a ligand-binding immunoblot assay and fluorescence microscopy. The polypeptide containing the carboxy (C)-terminal hydrophilic domain exhibited direct binding to INT-407 cells. Therefore, the C-terminal domain of IlpA allows this protein to be an adhesion molecule of V. vulnificus.
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