Cysteine-free cone snail venom peptides: Classification of precursor proteins and identification of mature peptides.

Autor: Vijayasarathy M; National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India., Kumar S; National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India.; Trivedi School of Biosciences, Ashoka University, Sonipat, India., Das R; National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India.; Department of Biochemistry and Bioinformatics, GITAM School of Science, GITAM (Deemed to be) University, Visakhapatnam, India., Balaram P; National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India.
Jazyk: angličtina
Zdroj: Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2024 Apr; Vol. 30 (4), pp. e3554. Date of Electronic Publication: 2023 Nov 27.
DOI: 10.1002/psc.3554
Abstrakt: The cysteine-free acyclic peptides present in marine cone snail venom have been much less investigated than their disulfide bonded counterparts. Precursor protein sequences derived from transcriptomic data, together with mass spectrometric fragmentation patterns for peptides present in venom duct tissue extracts, permit the identification of mature peptides. Twelve distinct gene superfamiles have been identified with precursor lengths between 64 and 158 residues. In the case of Conus monile, three distinct mature peptides have been identified, arising from two distinct protein precursors. Mature acyclic peptides are often post-translationally modified, with C-terminus amidation, a feature characteristic of neuropeptides. In the present study, 20 acyclic peptides from Conus monile and Conus betulinus were identified. The common modifications of C-terminus amidation, gamma carboxylation of glutamic acid (E to ϒ), N-terminus conversion of Gln (Q) to a pyroglutamyl residue (Z), and hydroxylation of Pro (P) to Hyp (O) are observed in one or more peptides identified in this study. Proteolytic trimming of sequences by cleavage at the C-terminus of Asn (N) residues is established. The presence of an asparagine endopeptidase is strengthened by the identification of legumain-like sequences in the transcriptome assemblies from diverse Conus species. Such sequences may be expected to have a cleavage specificity at Asn-Xxx peptide bonds.
(© 2023 European Peptide Society and John Wiley & Sons, Ltd.)
Databáze: MEDLINE
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