Antimicrobial proteins : from old proteins, new tricks
MetadataShow full item record
This review describes the main types of antimicrobial peptides (AMPs) synthesised by crustaceans, primarily those identified in shrimp, crayfish, crab and lobster. It includes an overview of their range of microbicidal activities and the current landscape of our understanding of their gene expression patterns in different body tissues. It further summarises how their expression might change following various types of immune challenges. Included in the review are proteins or protein fragments that have antimicrobial properties but are more usually associated with other biological functions, or are derived from such proteins. It discusses how these unconventional AMPs might be generated at, or delivered to, sites of infection and how they might contribute to crustacean host defence in vivo. It also highlights recent work that is starting to reveal the extent of multi-functionality displayed by some decapod AMPs, particularly their participation in other aspects of host protection. Examples of such activities include proteinase inhibition, phagocytosis, antiviral activity and haematopoiesis.
Smith , V & Dyrynda , E 2015 , ' Antimicrobial proteins : from old proteins, new tricks ' Molecular Immunology , vol 68 , no. Issue 2, Part B , pp. 383-398 . DOI: 10.1016/j.molimm.2015.08.009
© 2015. Elsevier Ltd. All rights reserved. This is the author’s version of a work that was accepted for publication in Molecular Immunology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Molecular Immunology, 29/08/2015, http://dx.doi.org/10.1016/j.molimm.2015.08.009
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.