Abstract
Bacterial surface proteins constitute an amazing repertoire of molecules with important functions such as adherence, invasion, signalling and interaction with the host immune system or environment. In Gram-positive bacteria, many surface proteins of the “LPxTG” family are anchored to the peptidoglycan (PG) by an enzyme named sortase. While this anchoring mechanism has been clearly deciphered, less is known about the spatial organization of cell wall-anchored proteins in the bacterial envelope. Here, we review the question of the precise spatial and temporal positioning of LPxTG proteins in subcellular domains in spherical and ellipsoid bacteria (Staphylococcus aureus, Streptococcus pyogenes, Streptococcus agalactiae and Enterococcus faecalis) and in the rod-shaped bacterium Listeria monocytogenes. Deposition at specific sites of the cell wall is a dynamic process tightly connected to cell division, secretion, cell morphogenesis and levels of gene expression. Studying spatial occupancy of these cell wall-anchored proteins not only provides information on PG dynamics in responses to environmental changes, but also suggests that pathogenic bacteria control the distribution of virulence factors at specific sites of the surface, including pole, septa or lateral sites, during the infectious process.
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Acknowledgments
We thank Nienke Buddelmeijer for critical reading of the manuscript. H. Bierne acknowledges supports from the French National Research Agency (ANR 11-BSV3-0003 EPILIS) and the iXcore Foundation for Research.
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© 2016 Springer International Publishing Switzerland
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Dramsi, S., Bierne, H. (2016). Spatial Organization of Cell Wall-Anchored Proteins at the Surface of Gram-Positive Bacteria. In: Bagnoli, F., Rappuoli, R. (eds) Protein and Sugar Export and Assembly in Gram-positive Bacteria . Current Topics in Microbiology and Immunology, vol 404. Springer, Cham. https://doi.org/10.1007/82_2016_4
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DOI: https://doi.org/10.1007/82_2016_4
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