PXD056545

PXD056545 is an original dataset announced via ProteomeXchange.

Title	An ancient lysozyme in placozoans
Description	Lysozymes are an essential part of nutrition and antibacterial immunity in metazoans, executing the breakdown of bacterial cell walls via the hydrolysis of peptidoglycan. Although various lysozymes have been reported for several bilaterian phyla, the origin of metazoan lysozymes remains elusive as they seemed to lack in non-bilaterian animals. In this study, we investigated a putative goose-type lysozyme (PLys, glycoside hydrolase family 23, GH23) of the placozoan Trichoplax sp. H2 which we localized in gland cells of the ventral epithelium. N-terminal of the conserved GH23 lysozyme domain, PLys contains a non-conserved cysteine-rich domain. We could show truncation of this N-terminal domain in maturation process of PLys and a drastic increase in enzymatic activity at the cost of stability using recombinantly expressed physiological proteoforms of PLys. Phylogenetic analysis of GH23 lysozymes from all domains of life revealed a monophyletic radiation in animals. Based on structural comparisons and their distribution in the animal tree of life, metazoan g-type GH23 lysozymes appear to have originated from a horizontal gene transfer event from bacteria to an early pre-bilaterian ancestor. GH23 lysozymes have then been retained and expanded in many phyla, including Porifera, Cnidaria, Placozoa and chordates acting as key component in the antibacterial arsenal since early metazoan evolution.
HostingRepository	PRIDE
AnnounceDate	2025-11-14
AnnouncementXML	Submission_2025-11-14_02:16:52.468.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Andreas Tholey
SpeciesList	scientific name: Trichoplax sp. H2; NCBI TaxID: NEWT:287889;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos; Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2024-10-07 06:29:21	ID requested
⏵ 1	2025-11-14 02:16:53	announced

Dataset with its publication pending

submitter keyword: lyozyme, pacozoan, trucnated

Prof. Dr. Andreas Tholey
contact affiliation	Institut für Experimentelle Medizin (IEM) Arbeitsgruppe Systematische Proteomforschung Christian-Albrechts-Universität zu Kiel Kiel, Germany
contact email	a.tholey@iem.uni-kiel.de
lab head
Andreas Tholey
contact affiliation	Systematic Proteome Research & Bioanalytics, University of Kiel
contact email	a.tholey@iem.uni-kiel.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD056545
     1. Label: PRIDE project
     2. Name: An ancient lysozyme in placozoans