Pneumolysin-damaged cells benefit from non-homogeneous toxin binding to cholesterol-rich membrane domains.

Drücker, Patrick; Bachler, Simon; Wolfmeier, Heidi Annemarie; Schönauer, Roman; Köffel, René; Babiychuk, Viktoria S; Dittrich, Petra S; Draeger, Annette; Babiychuk, Eduard (2018). Pneumolysin-damaged cells benefit from non-homogeneous toxin binding to cholesterol-rich membrane domains. Biochimica and biophysica acta - molecular and cell biology of lipids, 1863(8), pp. 795-805. Elsevier 10.1016/j.bbalip.2018.04.010

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Nucleated cells eliminate lesions induced by bacterial pore-forming toxins, such as pneumolysin via shedding patches of damaged plasmalemma into the extracellular milieu. Recently, we have shown that the majority of shed pneumolysin is present in the form of inactive pre-pores. This finding is surprising considering that shedding is triggered by Ca-influx following membrane perforation and therefore is expected to positively discriminate for active pores versus inactive pre-pores. Here we provide evidence for the existence of plasmalemmal domains that are able to attract pneumolysin at high local concentrations. Within such a domain an immediate plasmalemmal perforation induced by a small number of pneumolysin pores would be capable of triggering the elimination of a large number of not yet active pre-pores/monomers and thus pre-empt more frequent and perilous perforation events. Our findings provide further insights into the functioning of the cellular repair machinery which benefits from an inhomogeneous plasmalemmal distribution of pneumolysin.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy > Cell Biology

UniBE Contributor:

Drücker, Patrick; Wolfmeier, Heidi Annemarie; Schönauer, Roman; Köffel, René; Draeger, Annette and Babiychuk, Eduard

Subjects:

600 Technology > 610 Medicine & health

ISSN:

1388-1981

Publisher:

Elsevier

Language:

English

Submitter:

Annette Draeger

Date Deposited:

20 Feb 2019 10:33

Last Modified:

05 Nov 2019 13:18

Publisher DOI:

10.1016/j.bbalip.2018.04.010

PubMed ID:

29679741

BORIS DOI:

10.7892/boris.125165

URI:

https://boris.unibe.ch/id/eprint/125165

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