Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/134683
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Type: | Journal article |
Title: | Periscope Proteins are variable-length regulators of bacterial cell surface interactions |
Author: | Whelan, F. Lafita, A. Gilburt, J. Dégut, C. Griffiths, S.C. Jenkins, H.T. St John, A.N. Paci, E. Moir, J.W.B. Plevin, M.J. Baumann, C.G. Bateman, A. Potts, J.R. |
Citation: | Proceedings of the National Academy of Sciences of USA, 2021; 118(23):e2101349118-1-e2101349118-10 |
Publisher: | Proceedings of the National Academy of Sciences |
Issue Date: | 2021 |
ISSN: | 0027-8424 1091-6490 |
Statement of Responsibility: | Fiona Whelan, Aleix Lafita, James Gilburt, Clément Dégut, Samuel C. Griffiths, Huw T. Jenkins, Alexander N. St John, Emanuele Paci, James W. B. Moir, Michael J. Plevin, Christoph G. Baumann, Alex Bateman, and Jennifer R. Potts |
Abstract: | Changes at the cell surface enable bacteria to survive in dynamic environments, such as diverse niches of the human host. Here, we reveal “Periscope Proteins” as a widespread mechanism of bacterial surface alteration mediated through protein length variation. Tandem arrays of highly similar folded domains can form an elongated rod-like structure; thus, variation in the number of domains determines how far an N-terminal host ligand binding domain projects from the cell surface. Supported by newly available long-read genome sequencing data, we propose that this class could contain over 50 distinct proteins, including those implicated in host colonization and biofilm formation by human pathogens. In large multidomain proteins, sequence divergence between adjacent domains appears to reduce interdomain misfolding. Periscope Proteins break this “rule,” suggesting that their length variability plays an important role in regulating bacterial interactions with host surfaces, other bacteria, and the immune system. |
Keywords: | protein structure; bacterial surface proteins; multidomain proteins |
Description: | Published May 31, 2021. |
Rights: | Copyright © 2021 the Author(s). Published by PNAS. This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY). |
DOI: | 10.1073/pnas.2101349118 |
Published version: | http://dx.doi.org/10.1073/pnas.2101349118 |
Appears in Collections: | Molecular and Biomedical Science publications |
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hdl_134683.pdf | Published version | 1.64 MB | Adobe PDF | View/Open |
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