Hyaluronan breakdown by snake venom hyaluronidases: From toxins delivery to immunopathology

França, Felipe Silva de; Tambourgi, Denise V.

doi:10.3389/fimmu.2023.1125899

Cited by 2 publications

(1 citation statement)

References 62 publications

(77 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The hyaluronidase from Eulalia has higher homology matches with hyaluronidases from highly venomous snakes. In these animals, hyaluronidases have inflammatory actions due to the degradation of products and the generation of hyaluronan fragments, and thus proving the importance of hyaluronidase in envenomation studies [45]. This enzyme shows lower levels of sequence diversity than other toxins across animal taxa [46].…”

Section: Discussionmentioning

confidence: 99%

Exploration of Toxins from a Marine Annelid: An Analysis of Phyllotoxins and Accompanying Bioactives

Rodrigo,

Moutinho Cabral,

Alexandre

et al. 2024

Animals

View full text Add to dashboard Cite

Proteinaceous toxins are peptides or proteins that hold great biotechnological value, evidenced by their ecological role, whether as defense or predation mechanisms. Bioprospecting using bioinformatics and omics may render screening for novel bioactives more expeditious, especially considering the immense diversity of toxin-secreting marine organisms. Eulalia sp. (Annelida: Phyllodocidae), a toxin bearing marine annelid, was recently shown to secrete cysteine-rich protein (Crisp) toxins (hitherto referred to as ‘phyllotoxins’) that can immobilize its prey. By analyzing and validating transcriptomic data, we narrowed the list of isolated full coding sequences of transcripts of the most abundant toxins or accompanying bioactives secreted by the species (the phyllotoxin Crisp, hyaluronidase, serine protease, and peptidases M12A, M13, and M12B). Through homology matching with human proteins, the biotechnological potential of the marine annelid’s toxins and related proteins was tentatively associated with coagulative and anti-inflammatory responses for the peptidases PepM12A, SePr, PepM12B, and PepM13, and with the neurotoxic activity of Crisp, and finally, hyaluronidase was inferred to bear properties of an permeabilizing agent. The in silico analysis succeeded by validation by PCR and Sanger sequencing enabled us to retrieve cDNAs can may be used for the heterologous expression of these toxins.

show abstract

Section: Discussionmentioning

confidence: 99%