Bosso, Andrea (2017) Human and plant proteins as reservoirs of host defence peptides. [Tesi di dottorato]

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Item Type: Tesi di dottorato
Lingua: English
Title: Human and plant proteins as reservoirs of host defence peptides
Creators:
CreatorsEmail
Bosso, Andreaandrea.bosso@unina.it
Date: 7 December 2017
Number of Pages: 95
Institution: Università degli Studi di Napoli Federico II
Department: dep03
Dottorato: phd007
Ciclo di dottorato: 30
Coordinatore del Corso di dottorato:
nomeemail
Cozzolino, Salvatorecozzolin@unina.it
Tutor:
nomeemail
Pizzo, ElioUNSPECIFIED
Date: 7 December 2017
Number of Pages: 95
Uncontrolled Keywords: Antimicrobial peptides, host defence peptides, immunomodulation,anti-biofilm, GVF27, cryptides.
Settori scientifico-disciplinari del MIUR: Area 05 - Scienze biologiche > BIO/10 - Biochimica
Date Deposited: 09 Jan 2018 12:53
Last Modified: 09 Apr 2019 10:51
URI: http://www.fedoa.unina.it/id/eprint/12077

Abstract

Antimicrobial peptides (AMPs), known also as host defense peptides, are fundamental evolutionarily conserved components of innate immunity. Constitutively or inducibly expressed in response to invasion by pathogens, they operate synergistically with other defence molecules to combat infections. Despite differences in their size and sequence, many of them share a net positive charge at neutral pH, and fold into amphipathic structures, often after contact with bacterial surfaces. HDPs are attractive alternative candidates for antibiotic treatment, because they offer several advantages over the currently used drugs. They combat pathogens by targeting bacterial membranes, thus impairing essential membrane-related functions, and, in some cases, also target intracellular components. Due to their peculiar mechanism, the resistance towards these peptides would be difficult for the bacteria to develop. Several proteins, including proteins apparently not involved in immunity, can behave as sources of HDPs hidden in their primary structures and released by the action of host and/or bacterial proteases. Recently it has been developed a bioinformatic tool allowing to identify such “cryptic HDPs”. Analyzing a library of 4000 proteins, we have identified and studied several novel cryptic HDPs from human and plant. Among these, three human peptides (GVF27, ApoBS and ApoBL) show pharmacologically relevant properties like significant antimicrobial activity on a broad spectrum of bacteria (including some clinical isolates), very promising antibiofilm properties (both on pre-formed and attached biofilm), strong affinity for endotoxins as LPS and LTA and immunomodulatory properties on LPS induced murine macrophages, while two peptides from plant (IKY31 and IKY23) are strong anti-biofilm agents and not toxic against eukaryotic cells. Overall our data suggest that these new cryptic HDPs, could serve as leads for the design of innovative antimicrobials with immunostimulating and immunomodulatory properties.

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