4.5 Article

Shigella viruses Sf22 and KRT47 require outer membrane protein C for infection

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1864, Issue 7, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.bbamem.2022.183920

Keywords

Bacteriophage; Shigella; Phage therapy; phage-host interactions; outer membrane protein C

Funding

  1. National Institutes of Health [GM110185]
  2. National Science Foundation CAREER Award [1750125]
  3. University of Florida
  4. Div Of Molecular and Cellular Bioscience
  5. Direct For Biological Sciences [1750125] Funding Source: National Science Foundation

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Viruses rely on hosts for replication, so identifying suitable host cells is a critical step in the infection process. Bacterial viruses, or phages, use receptor binding proteins to distinguish between susceptible and non-susceptible hosts. Bacteria with modified or deleted receptor genes often undergo positive selection in the presence of phages, and this can have various effects on the bacteria's phenotype.
Viruses rely on hosts for their replication: thus, a critical step in the infection process is identifying a suitable host cell. Bacterial viruses, known as bacteriophages or phages, often use receptor binding proteins to discriminate between susceptible and non-susceptible hosts. By being able to evade predation, bacteria with modified or deleted receptor-encoding genes often undergo positive selection during growth in the presence of phage. Depending on the specific receptor(s) a phage uses, this may subsequently affect the bacteria's ability to form biofilms, its resistance to antibiotics, pathogenicity, or its phenotype in various environments. In this study, we characterize the interactions between two T4-like phages, Sf22 and KRT47, and their host receptor S. flexneri outer membrane protein C (OmpC). Results indicate that these phages use a variety of surface features on the protein, and that complete resistance most frequently occurs when hosts delete the ompC gene in full, encode premature stop codons to prevent OmpC synthesis, or eliminate specific regions encoding exterior loops.

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