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ORIGINAL RESEARCH article

Front. Mol. Biosci.

Sec. Structural Biology

Identification of lysozyme in Venetin-1 nanoparticle from the coelomic fluid of the earthworm Dendrobaena veneta

Provisionally accepted
Marta  Julia FiołkaMarta Julia Fiołka1*Magdalena  DryglewskaMagdalena Dryglewska2Kinga  LewtakKinga Lewtak1Michał  RawskiMichał Rawski3Tomasz  BuchwaldTomasz Buchwald4Ewa  SkwarekEwa Skwarek1Sachin  KoteSachin Kote5Jakub  FaktorJakub Faktor5Weronika  Ścibek-RejmontowskaWeronika Ścibek-Rejmontowska5Paulina  CzaplewskaPaulina Czaplewska5Wojciech  KaźmierskiWojciech Kaźmierski6
  • 1Uniwersytet Marii Curie-Sklodowskiej, Lublin, Poland
  • 2Uniwersytet Medyczny w Lublinie, Lublin, Poland
  • 3Uniwersytet Jagiellonski w Krakowie, Kraków, Poland
  • 4Politechnika Poznanska, Poznań, Poland
  • 5Uniwersytet Gdanski, Gdańsk, Poland
  • 6Bruker Polska Sp. z o.o., Poznań, Poland

The final, formatted version of the article will be published soon.

In the present study, lysozyme was analyzed in the nanoparticle Venetin-1 obtained from the coelomic fluid (CF) of the earthworm Dendrobaena veneta. Venetin-1 is a protein-polysaccharide complex and has proven anti-cancer (non-small lung cancer, colon cancer, cervical cancer), antifungal and immunostimulating properties. The lysozyme-type activity in this compound was significantly higher than in the crude CF. The analysis showed the highest concentration of lysozyme recognized by antibodies directed against human lysozyme is in the fraction containing compounds with a mass above 100 kDa and in the preparation obtained using a cut-off point of 6-8 kDa. Raman analysis showed a significant similarity of the protein part of Venetin-1 and EWL. FTIR analyses confirmed that the preparation obtained under these conditions showed high similarity to egg white lysozyme (EWL). Cryo-EM studies revealed the structure of the tested nanoparticle containing both lysozyme and lysenin fragments. Immunoblotting using antibodies directed against human lysozyme revealed proteins of mass 11, 33, 44, 88 and 132 kDa recognized in Venetin-1. Proteomic analyses confirmed the presence of these proteins and similarity to human lysozyme. These observations suggest the presence of polymeric forms of lysozyme in the tested complex, and zeta potential analysis revealed properties of the nanoparticle that predispose it to use in medicine.

Keywords: Venetin-1, earthworms, Coelomic fluid, lysozyme, lysenine, Immunodetection

Received: 06 Oct 2025; Accepted: 07 Nov 2025.

Copyright: © 2025 Fiołka, Dryglewska, Lewtak, Rawski, Buchwald, Skwarek, Kote, Faktor, Ścibek-Rejmontowska, Czaplewska and Kaźmierski. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

* Correspondence: Marta Julia Fiołka, marta.fiolka@mail.umcs.pl

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