PXD037610

PXD037610 is an original dataset announced via ProteomeXchange.

Title	Asp caterpillar (Megalopyge ssp.) venom proteomes
Description	Larvae of the genus Megalopyge (Lepidoptera: Zygaenoidea: Megalopygidae), called asp or puss caterpillars, produce defensive venoms that cause severe acute pain. Here, we present the anatomy, chemistry, and mode of action of the venom systems of caterpillars of two megalopygid species, the Southern flannel moth Megalopyge opercularis and the black-waved flannel moth Megalopyge crispata. We show that megalopygid venom is produced in secretory cells that lie beneath the cuticle and are connected to the venom spines by canals. Megalopygid venoms consist of larger aerolysin-like pore-forming toxins, which we have named megalysins, and a small number of peptides. Venom potently activates mammalian sensory neurons via membrane permeabilization and causes sustained spontaneous pain behaviours and paw swelling in mice. These bioactivities can be easily ablated by treatment with heat, organic solvents, or proteases, suggesting they are mediated by larger proteins, most likely the megalysins. We show that the megalysins were recruited as venom toxins in the Megalopygidae following horizontal transfer of genes from bacteria to the ancestors of Lepidoptera. The megalopygid venom system differs markedly from those of previously studied venomous zygaenoids of the family Limacodidae, suggestive of independent origins. Megalopygids have recruited aerolysin-like proteins as venom toxins convergently with centipedes, cnidarians, and fish. This study highlights the role of horizontal gene transfer in venom evolution.
HostingRepository	PRIDE
AnnounceDate	2024-01-26
AnnouncementXML	Submission_2024-01-26_06:44:26.158.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Andrew Walker
SpeciesList	scientific name: Megalopyge opercularis; NCBI TaxID: 1113279;
ModificationList	amidated residue
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2022-10-20 02:51:24	ID requested
⏵ 1	2024-01-26 06:44:26	announced

Walker AA, Robinson SD, Merritt DJ, Cardoso FC, Goudarzi MH, Mercedes RS, Eagles DA, Cooper P, Zdenek CN, Fry BG, Hall DW, Vetter I, King GF, Horizontal gene transfer underlies the painful stings of asp caterpillars (Lepidoptera: Megalopygidae). Proc Natl Acad Sci U S A, 120(29):e2305871120(2023) [pubmed]

10.1073/pnas.2305871120;

ProteomeXchange project tag: Toxicoproteomics (B/D-HPP), Biology/Disease-Driven Human Proteome Project (B/D-HPP), Human Proteome Project

submitter keyword: Megalopyge, venom,Lepidoptera, Megalopygidae

Glenn F. King
contact affiliation	Institute for Molecular Biosciences, The University of Queensland
contact email	glenn.king@imb.uq.edu.au
lab head
Andrew Walker
contact affiliation	University of Queensland
contact email	a.walker@uq.edu.au
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/01/PXD037610

PRIDE project URI

• PRIDE
  1. PXD037610
     1. Label: PRIDE project
     2. Name: Asp caterpillar (Megalopyge ssp.) venom proteomes