Periscope Proteins are variable-length regulators of bacterial cell surface interactions.

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 int

SUBMITTER: Whelan F 

PROVIDER: S-EPMC8201768 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature