Abstract
Escherichia coli is a versatile pathogen causing millions of infections in humans every year. This bacterium can form multicellular aggregates when it expresses a self-associating protein, antigen 43 (Ag43), on its surface. We have discovered that Ag43-expressing E. coli cells are efficiently taken up by human defense cells, polymorphonuclear neutrophils (PMNs), in an opsonin-independent manner. Surprisingly, the phagocytosed bacteria were not immediately killed but resided as tight aggregates within the PMNs. Our observations indicate that Ag43-mediated uptake and survival in PMNs constitute a mechanism to subvert one of the primary defense mechanisms of the human body.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adhesins, Bacterial / immunology
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Adhesins, Bacterial / metabolism*
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Adhesins, Escherichia coli
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Antigens, Bacterial / immunology
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Antigens, Bacterial / metabolism*
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Bacterial Outer Membrane Proteins / immunology
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Bacterial Outer Membrane Proteins / metabolism*
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Cells, Cultured
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Escherichia coli / immunology*
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Escherichia coli Infections / immunology
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Escherichia coli Proteins / immunology
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Escherichia coli Proteins / metabolism*
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Humans
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Neutrophils / immunology
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Neutrophils / microbiology*
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Phagocytosis / physiology
Substances
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Adhesins, Bacterial
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Adhesins, Escherichia coli
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Antigens, Bacterial
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Bacterial Outer Membrane Proteins
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Escherichia coli Proteins
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antigen 43, E coli