Glycerids are marine annelids commonly known as bloodworms. Bloodworms have an eversible proboscis adorned with jaws connected to venom glands. Bloodworms prey on invertebrates, and it is known that the venom glands produce compounds that can induce toxic effects in animals. Yet, none of these putative toxins has been characterized on a molecular basis. Here we present the transcriptomic profiles of the venom glands of three species of bloodworm, Glycera dibranchiata, Glycera fallax and Glycera tridactyla, as well as the body tissue of G. tridactyla. The venom glands express a complex mixture of transcripts coding for putative toxin precursors. These transcripts represent 20 known toxin classes that have been convergently recruited into animal venoms, as well as transcripts potentially coding for Glycera-specific toxins. The toxins represent five functional categories: Pore-forming and membrane-disrupting toxins, neurotoxins, protease inhibitors, other enzymes, and CAP domain toxins. Many of the transcripts coding for putative Glycera toxins belong to classes that have been widely recruited into venoms, but some are homologs of toxins previously only known from the venoms of scorpaeniform fish and monotremes (stonustoxin-like toxin), turrid gastropods (turripeptide-like peptides), and sea anemones (gigantoxin I-like neurotoxin). This complex mixture of toxin homologs suggests that bloodworms employ venom while predating on macroscopic prey, casting doubt on the previously widespread opinion that G. dibranchiata is a detritivore. Our results further show that researchers should be aware that different assembly methods, as well as different methods of homology prediction, can influence the transcriptomic profiling of venom glands.
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http://dx.doi.org/10.1093/gbe/evu190 | DOI Listing |
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January 2025
Department of Biology, School of Science, Shahid Chamran University of Ahvaz, Ahvaz, Iran. Electronic address:
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December 2024
Key Laboratory of Genetic Evolution & Animal Models, Engineering Laboratory of Peptides of Chinese Academy of Sciences, Key Laboratory of Bioactive Peptides of Yunnan Province, KIZ-CUHK Joint Laboratory of Bioresources and Molecular Research in Common Diseases, National Resource Center for Non-Human Primates, and Sino-African Joint Research Center, New Cornerstone Science Laboratory, Kunming Institute of Zoology, The Chinese Academy of Sciences, Kunming 650201, China.
The venoms of Theraphosidae spiders have evolved into diverse natural pharmacopeias through selective pressures. is a global health threat that frequently causes life-threatening meningitis and fungemia, particularly in immunocompromised patients. In this study, we identify a novel anti- peptide, QS18 (QCFKVCFRKRCFTKCSRS), from the venom gland of China's native spider species by utilizing bioinformatic tools.
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November 2024
Department of Life Science, Dongguk University-Seoul, Goyang 10326, Republic of Korea.
Trans R Soc Trop Med Hyg
January 2025
Department of Radiodiagnosis, Dr RPGMC, Tanda, Kangra (HP) India 176001.
We describe a series of five patients with bilateral parotid enlargement as a sequalae to envenomation by the common krait (Bungarus caeruleus). Fine-needle aspiration cytology of the parotid gland was performed in four cases. The cytology revealed a mild lymphocytic inflammatory response in a red blood cell mixed proteinaceous background.
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November 2024
Facultad de Ciencias Exactas y Naturales, Pontificia Universidad Católica del Ecuador, Quito 170525, Ecuador.
Previous proteomic studies of viperid venom revealed that it is mainly composed of metalloproteinases (SVMPs), serine proteinases (SVSPs), phospholipase A2 (PLA2), and C-type lectins (CTLs). However, other proteins appear in minor amounts that affect prey and need to be identified. This study aimed to identify novel toxic proteins in the venom gland transcriptome of and , using data from NCBI.
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