Killer Peptide: an antibody-derived self-assembling peptide bridging antimicrobial and host-defense mechanisms

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dc.contributor.authorFernandez de Ullivarri, Miguel
dc.contributor.authorO’Sullivan, Colin
dc.contributor.authorRoss, R. Paul
dc.contributor.authorHill, Colin
dc.contributor.funderTaighde Éireann - Research Ireland
dc.date.accessioned2026-09-08T11:21:01Z
dc.date.available2026-09-08T11:21:01Z
dc.date.issued2026-06-18
dc.description.abstractAntimicrobial resistance and persistent biofilm-associated infections continue to drive the search for peptide-based anti-infective agents with mechanisms distinct from conventional antibiotics. Killer Peptide (KP) is an antibody-derived decapeptide originally identified through yeast killer toxin mimicry studies and has emerged as a distinctive example of a multifunctional bioactive peptide. Experimental studies have reported particularly strong antifungal activity, together with activity against selected bacteria, biofilms, viruses, and protozoa, as well as immunomodulatory effects in preclinical models. Mechanistically, KP appears to act through a multistep process involving target-surface recognition, cellular internalization, induction of intracellular stress pathways, and reversible self-assembly into fibrillar structures that may support localized peptide retention. In parallel, KP has been reported to influence innate and adaptive immune responses, suggesting potential host-defense-enhancing properties. In this review, we critically reassess two decades of KP research, covering its molecular origin, structural features, antimicrobial spectrum, mechanisms of action, engineered derivatives, and translational prospects. We also examine current limitations, including the relatively narrow evidence base, incomplete pharmacological characterization, and the need for independent validation across disease models. KP represents a useful conceptual framework for the development of next-generation multifunctional peptides integrating antimicrobial, pathogen-triggered assembly, and immunomodulatory properties.en
dc.description.sponsorshipTaighde Éireann - Research Ireland|SFI/12/RC/2273_P2
dc.description.versionPublished Version
dc.format.extent16
dc.format.mimetypeapplication/pdfen
dc.identifier.articleidfuag026
dc.identifier.authororcidFernandez de Ullivarri, Miguel
dc.identifier.authororcidO’Sullivan, Colin
dc.identifier.authororcidRoss, R. Paul§0000-0003-4876-8839
dc.identifier.authororcidHill, Colin§0000-0002-8527-1445
dc.identifier.citationFernandez de Ullivarri, M, O’Sullivan, C, Ross, R P & Hill, C 2026, 'Killer Peptide: an antibody-derived self-assembling peptide bridging antimicrobial and host-defense mechanisms', FEMS Microbiology Reviews, vol. 50, fuag026, pp. 1-16. https://doi.org/10.1093/femsre/fuag026
dc.identifier.doi10.1093/femsre/fuag026
dc.identifier.endpage16
dc.identifier.issn0168-6445
dc.identifier.otherORCID: /0000-0003-4876-8839/work/226165570
dc.identifier.otherORCID: /0000-0002-8527-1445/work/226165912
dc.identifier.startpage1
dc.identifier.urihttps://hdl.handle.net/10468/19187
dc.identifier.volume50
dc.language.isoen
dc.publisherOxford University Press
dc.relation.urihttps://www.scopus.com/pages/publications/105042496834
dc.rights© 2026, the Author(s) . Published by Oxford University Press on behalf of FEMS. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
dc.rights.accessrightsopen access
dc.rights.licensenameAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.statusPeer reviewed
dc.subjectAnti-idiotypic antibodies
dc.subjectImmunomodulation
dc.subjectMulti-kingdom activity
dc.subjectPeptide self-assembly
dc.subjectProgrammed cell death
dc.subjectβ-glucan recognition
dc.subject[APCMicrobiome]
dc.subject[Microbiology]
dc.titleKiller Peptide: an antibody-derived self-assembling peptide bridging antimicrobial and host-defense mechanismsen
dc.typeReview
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