Issue 7, 2017

Proline-rich antimicrobial peptides targeting protein synthesis

Abstract

Covering: up to 2017

The innate immune system employs a broad array of antimicrobial peptides (AMPs) to attack invading microorganisms. While most AMPs act by permeabilizing the bacterial membrane, specific subclasses of AMPs have been identified that pass through membranes and inhibit bacterial growth by targeting fundamental intracellular processes. One such subclass is the proline-rich antimicrobial peptides (PrAMPs) that bind to the ribosome and interfere with the process of protein synthesis. A diverse range of PrAMPs have been identified in insects, such as bees, wasps and beetles, and crustaceans, such as crabs, as well as in mammals, such as cows, sheep, goats and pigs. Mechanistically, the best-characterized PrAMPs are the insect oncocins, such as Onc112, and bovine bactenecins, such as Bac7. Biochemical and structural studies have revealed that these PrAMPs bind within the ribosomal exit tunnel with a reverse orientation compared to a nascent polypeptide chain. The PrAMPs allow initiation but prevent the transition into the elongation phase of translation. Insight into the interactions of PrAMPs with their ribosomal target provides the opportunity to further develop these peptides as novel antimicrobial agents.

Graphical abstract: Proline-rich antimicrobial peptides targeting protein synthesis

Article information

Article type
Highlight
Submitted
24 ማርች 2017
First published
24 ሜይ 2017

Nat. Prod. Rep., 2017,34, 702-711

Proline-rich antimicrobial peptides targeting protein synthesis

M. Graf, M. Mardirossian, F. Nguyen, A. C. Seefeldt, G. Guichard, M. Scocchi, C. A. Innis and D. N. Wilson, Nat. Prod. Rep., 2017, 34, 702 DOI: 10.1039/C7NP00020K

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements