Mycoplasma pneumoniae CARDS Toxin Is Internalized via Clathrin-Mediated Endocytosis

Manickam Krishnan; T. R. Kannan; Joel B. Baseman

doi:10.1371/journal.pone.0062706

Mycoplasma pneumoniae CARDS Toxin Is Internalized via Clathrin-Mediated Endocytosis

Manickam Krishnan, T. R. Kannan, Joel B. Baseman

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

Bacterial toxins possess specific mechanisms of binding and uptake by mammalian cells. Mycoplasma pneumoniae CARDS (Community Acquired Respiratory Distress Syndrome) toxin is a 68 kDa protein, which demonstrates high binding affinity to human surfactant protein-A and exhibits specific biological activities including mono-ADP ribosylation and vacuolization. These properties lead to inflammatory processes in the airway and a range of cytopathologies including ciliostasis, loss of tissue integrity and injury, and cell death. However, the process by which CARDS toxin enters target cells is unknown. In this study, we show that CARDS toxin binds to mammalian cell surfaces and is internalized rapidly in a dose and time-dependent manner using a clathrin-mediated pathway, as indicated by inhibition of toxin internalization by monodansylcadaverine but not by methyl-β-cyclodextrin or filipin. Furthermore, the internalization of CARDS toxin was markedly inhibited in clathrin-depleted cells.

Original language	English (US)
Article number	e62706
Journal	PloS one
Volume	8
Issue number	5
DOIs	https://doi.org/10.1371/journal.pone.0062706
State	Published - May 7 2013

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Agricultural and Biological Sciences(all)
General

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abstract = "Bacterial toxins possess specific mechanisms of binding and uptake by mammalian cells. Mycoplasma pneumoniae CARDS (Community Acquired Respiratory Distress Syndrome) toxin is a 68 kDa protein, which demonstrates high binding affinity to human surfactant protein-A and exhibits specific biological activities including mono-ADP ribosylation and vacuolization. These properties lead to inflammatory processes in the airway and a range of cytopathologies including ciliostasis, loss of tissue integrity and injury, and cell death. However, the process by which CARDS toxin enters target cells is unknown. In this study, we show that CARDS toxin binds to mammalian cell surfaces and is internalized rapidly in a dose and time-dependent manner using a clathrin-mediated pathway, as indicated by inhibition of toxin internalization by monodansylcadaverine but not by methyl-β-cyclodextrin or filipin. Furthermore, the internalization of CARDS toxin was markedly inhibited in clathrin-depleted cells.",

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Mycoplasma pneumoniae CARDS Toxin Is Internalized via Clathrin-Mediated Endocytosis

Abstract

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