Structural highlights
Publication Abstract from PubMedChanges 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. Periscope Proteins are variable-length regulators of bacterial cell surface interactions.,Whelan F, Lafita A, Gilburt J, Degut C, Griffiths SC, Jenkins HT, St John AN, Paci E, Moir JWB, Plevin MJ, Baumann CG, Bateman A, Potts JR Proc Natl Acad Sci U S A. 2021 Jun 8;118(23). pii: 2101349118. doi:, 10.1073/pnas.2101349118. PMID:34074781[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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