Identification of LukPQ, a novel, equid-adapted leukocidin of Staphylococcus aureus
Koop, Gerrit; Vrieling, Manouk; Storisteanu, Daniel M L; Lok, Laurence S C; Monie, Tom; van Wigcheren, Glenn; Raisen, Claire; Ba, Xiaoliang; Gleadall, Nicholas; Hadjirin, Nazreen; Timmerman, Arjen J; Wagenaar, Jaap A; Klunder, Heleen M; Fitzgerald, J Ross; Zadoks, Ruth; Paterson, Gavin K; Torres, Carmen; Waller, Andrew S; Loeffler, Anette; Loncaric, Igor; Hoet, Armando E; Bergström, Karin; De Martino, Luisa; Pomba, Constança; de Lencastre, Hermínia; Ben Slama, Karim; Gharsa, Haythem; Richardson, Emily J; Chilvers, Edwin R; de Haas, Carla; van Kessel, Kok; van Strijp, Jos A G; Harrison, Ewan M; Holmes, Mark A
(2017) Scientific Reports, volume 7
(Article)
Abstract
Bicomponent pore-forming leukocidins are a family of potent toxins secreted by Staphylococcus aureus, which target white blood cells preferentially and consist of an S- and an F-component. The S-component recognizes a receptor on the host cell, enabling high-affinity binding to the cell surface, after which the toxins form a pore
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that penetrates the cell lipid bilayer. Until now, six different leukocidins have been described, some of which are host and cell specific. Here, we identify and characterise a novel S. aureus leukocidin; LukPQ. LukPQ is encoded on a 45 kb prophage (ΦSaeq1) found in six different clonal lineages, almost exclusively in strains cultured from equids. We show that LukPQ is a potent and specific killer of equine neutrophils and identify equine-CXCRA and CXCR2 as its target receptors. Although the S-component (LukP) is highly similar to the S-component of LukED, the species specificity of LukPQ and LukED differs. By forming non-canonical toxin pairs, we identify that the F-component contributes to the observed host tropism of LukPQ, thereby challenging the current paradigm that leukocidin specificity is driven solely by the S-component.
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Keywords: Bacteriology, Pathogens, Phage biology
ISSN: 2045-2322
Publisher: NLM (Medline)
(Peer reviewed)
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