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SNX3 drives maturation of Borrelia phagosomes by forming a hub for PI(3)P, Rab5a, and galectin-9

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SNX3 drives maturation of Borrelia phagosomes by forming a hub for PI(3)P, Rab5a, and galectin-9. / Klose, Matthias; Salloum, Johann Elias; Gonschior, Hannes; Linder, Stefan.

In: J CELL BIOL, Vol. 218, No. 9, 02.09.2019, p. 3039-3059.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Klose, M, Salloum, JE, Gonschior, H & Linder, S 2019, 'SNX3 drives maturation of Borrelia phagosomes by forming a hub for PI(3)P, Rab5a, and galectin-9', J CELL BIOL, vol. 218, no. 9, pp. 3039-3059. https://doi.org/10.1083/JCB.201812106

APA

Klose, M., Salloum, J. E., Gonschior, H., & Linder, S. (2019). SNX3 drives maturation of Borrelia phagosomes by forming a hub for PI(3)P, Rab5a, and galectin-9. J CELL BIOL, 218(9), 3039-3059. https://doi.org/10.1083/JCB.201812106

Vancouver

Klose M, Salloum JE, Gonschior H, Linder S. SNX3 drives maturation of Borrelia phagosomes by forming a hub for PI(3)P, Rab5a, and galectin-9. J CELL BIOL. 2019 Sep 2;218(9):3039-3059. https://doi.org/10.1083/JCB.201812106

Bibtex

@article{c9399267d2d34a409eebf67b4ad3ac98,
title = "SNX3 drives maturation of Borrelia phagosomes by forming a hub for PI(3)P, Rab5a, and galectin-9",
abstract = "The spirochete Borrelia burgdorferi, the causative agent of Lyme disease, is internalized by macrophages and processed in phagolysosomes. Phagosomal compaction, a crucial step in phagolysosome maturation, is driven by contact of Rab5a-positive vesicles with the phagosomal coat. We show that the sorting nexin SNX3 is transported with Rab5a vesicles and that its PX domain enables vesicle-phagosome contact by binding to PI(3)P in the phagosomal coat. Moreover, the C-terminal region of SNX3 recruits galectin-9, a lectin implicated in protein and membrane recycling, which we identify as a further regulator of phagosome compaction. SNX3 thus forms a hub for two distinct vesicle populations, constituting a convergence point for the endosomal recycling machinery, to contribute to phagosome maturation and intracellular processing of borreliae. These data also suggest that the helical shape of B. burgdorferi itself, providing sites of high curvature and thus local PI(3)P enrichment at phagosomes, may be one of the driving elements underlying the efficient elimination of spirochetes by immune cells.",
author = "Matthias Klose and Salloum, {Johann Elias} and Hannes Gonschior and Stefan Linder",
note = "{\textcopyright} 2019 Klose et al.",
year = "2019",
month = sep,
day = "2",
doi = "10.1083/JCB.201812106",
language = "English",
volume = "218",
pages = "3039--3059",
journal = "J CELL BIOL",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "9",

}

RIS

TY - JOUR

T1 - SNX3 drives maturation of Borrelia phagosomes by forming a hub for PI(3)P, Rab5a, and galectin-9

AU - Klose, Matthias

AU - Salloum, Johann Elias

AU - Gonschior, Hannes

AU - Linder, Stefan

N1 - © 2019 Klose et al.

PY - 2019/9/2

Y1 - 2019/9/2

N2 - The spirochete Borrelia burgdorferi, the causative agent of Lyme disease, is internalized by macrophages and processed in phagolysosomes. Phagosomal compaction, a crucial step in phagolysosome maturation, is driven by contact of Rab5a-positive vesicles with the phagosomal coat. We show that the sorting nexin SNX3 is transported with Rab5a vesicles and that its PX domain enables vesicle-phagosome contact by binding to PI(3)P in the phagosomal coat. Moreover, the C-terminal region of SNX3 recruits galectin-9, a lectin implicated in protein and membrane recycling, which we identify as a further regulator of phagosome compaction. SNX3 thus forms a hub for two distinct vesicle populations, constituting a convergence point for the endosomal recycling machinery, to contribute to phagosome maturation and intracellular processing of borreliae. These data also suggest that the helical shape of B. burgdorferi itself, providing sites of high curvature and thus local PI(3)P enrichment at phagosomes, may be one of the driving elements underlying the efficient elimination of spirochetes by immune cells.

AB - The spirochete Borrelia burgdorferi, the causative agent of Lyme disease, is internalized by macrophages and processed in phagolysosomes. Phagosomal compaction, a crucial step in phagolysosome maturation, is driven by contact of Rab5a-positive vesicles with the phagosomal coat. We show that the sorting nexin SNX3 is transported with Rab5a vesicles and that its PX domain enables vesicle-phagosome contact by binding to PI(3)P in the phagosomal coat. Moreover, the C-terminal region of SNX3 recruits galectin-9, a lectin implicated in protein and membrane recycling, which we identify as a further regulator of phagosome compaction. SNX3 thus forms a hub for two distinct vesicle populations, constituting a convergence point for the endosomal recycling machinery, to contribute to phagosome maturation and intracellular processing of borreliae. These data also suggest that the helical shape of B. burgdorferi itself, providing sites of high curvature and thus local PI(3)P enrichment at phagosomes, may be one of the driving elements underlying the efficient elimination of spirochetes by immune cells.

U2 - 10.1083/JCB.201812106

DO - 10.1083/JCB.201812106

M3 - SCORING: Journal article

VL - 218

SP - 3039

EP - 3059

JO - J CELL BIOL

JF - J CELL BIOL

SN - 0021-9525

IS - 9

ER -