Characterisation of a novel crustin isoform from mud crab, Scylla serrata (Forsskål, 1775) and its functional analysis in silico

S Neelima; M V Anju; V V Anooja; P P Athira; K Archana; S Muhammed Musthafa; Rosamma Philip

doi:10.1007/s40203-022-00138-w

Characterisation of a novel crustin isoform from mud crab, Scylla serrata (Forsskål, 1775) and its functional analysis in silico

In Silico Pharmacol. 2022 Dec 28;11(1):2. doi: 10.1007/s40203-022-00138-w. eCollection 2023.

Authors

S Neelima¹, M V Anju¹, V V Anooja¹, P P Athira¹, K Archana¹, S Muhammed Musthafa¹, Rosamma Philip¹

Affiliation

¹ Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, 682016 Kochi, Kerala India.

Abstract

A 336-base pair (bp) sized mRNA sequence encoding 111 amino acid size crustin isoform (MC-crustin) was obtained from the gill sample of the green mud crab, Scylla serrata. MC-crustin possessed an N-terminal signal peptide region comprising of 21 amino acid residues, followed by a 90 amino acid mature peptide region having a molecular weight of 10.164 kDa, charge + 4.25 and theoretical pI of 8.27. Sequence alignment and phylogenetic tree analyses revealed the peptide to be a Type I crustin, with four conserved cysteine residues forming the cysteine rich region, followed by WAP domain. MC-crustin was cationic with cysteine/proline rich structure and was predicted with antimicrobial, anti-inflammatory, anti-angiogenic and anti-hypertensive property making it a potential molecule for possible therapeutic applications.

Keywords: Antimicrobial peptide; Crustin; Mud-crab; Scylla serrata; WAP domain.

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