Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata

Antimicrobial peptides (AMPs) are the most common immune effectors in invertebrates that functions as the first line of defence against microbial infection. Scygonadin is an AMP which can be found in the seminal plasma of Scylla serrata. Preceding studies had shown that scygonadin have the ability...

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Main Authors:	Nurfarhana Rosli, Farah Ayunie Mohd Zain, Sandra Catherine Zainathan, Siti Nor Khadijah Addis
Format:	Article
Language:	English
Published:	Penerbit Universiti Kebangsaan Malaysia 2019
Online Access:	http://journalarticle.ukm.my/12781/ http://journalarticle.ukm.my/12781/ http://journalarticle.ukm.my/12781/1/48_01_14.pdf

id	ukm-12781
recordtype	eprints
spelling	ukm-127812019-04-16T09:07:59Z http://journalarticle.ukm.my/12781/ Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata Nurfarhana Rosli, Farah Ayunie Mohd Zain, Sandra Catherine Zainathan, Siti Nor Khadijah Addis, Antimicrobial peptides (AMPs) are the most common immune effectors in invertebrates that functions as the first line of defence against microbial infection. Scygonadin is an AMP which can be found in the seminal plasma of Scylla serrata. Preceding studies had shown that scygonadin have the ability to exhibit wide antimicrobial activities. Nonetheless, analysis of the antimicrobial properties of scygonadin is significantly dependent on acquiring sufficient amounts of the protein from mud crab, and this was proven difficult. Further functional studies of scygonadin and its commercial applications require a development of efficient, sustainable and cost-effective heterologous protein production. To address this issue, an expression plasmid containing 387 bp of scygonadin gene of Scylla serrata was cloned into pBAD/Myc-His A, expressed in TOP10 cells with L-arabinose as expression inducer, followed by protein purification by using immobilized metal affinity chromatography (IMAC). The optimal expression condition was determined by incubation with 0.02% of L-arabinose for 4 hours at 37°C. A total of 2 mg/ml of purified scygonadin with the molecular weight of ~17kDa was succesfully obtained. The results demonstrated that the recombinant scygonadin was successfully produced in heterologous expression system which may allow production of scygonadin in large quantities for further research and commercial application. Penerbit Universiti Kebangsaan Malaysia 2019-03 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/12781/1/48_01_14.pdf Nurfarhana Rosli, and Farah Ayunie Mohd Zain, and Sandra Catherine Zainathan, and Siti Nor Khadijah Addis, (2019) Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata. Malaysian Applied Biology, 48 (1). pp. 95-100. ISSN 0126-8643 http://mabjournal.com/index.php?option=com_content&view=article&id=897&catid=59:current-view&Itemid=56
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Kebangasaan Malaysia
building	UKM Institutional Repository
collection	Online Access
language	English
description	Antimicrobial peptides (AMPs) are the most common immune effectors in invertebrates that functions as the first line of defence against microbial infection. Scygonadin is an AMP which can be found in the seminal plasma of Scylla serrata. Preceding studies had shown that scygonadin have the ability to exhibit wide antimicrobial activities. Nonetheless, analysis of the antimicrobial properties of scygonadin is significantly dependent on acquiring sufficient amounts of the protein from mud crab, and this was proven difficult. Further functional studies of scygonadin and its commercial applications require a development of efficient, sustainable and cost-effective heterologous protein production. To address this issue, an expression plasmid containing 387 bp of scygonadin gene of Scylla serrata was cloned into pBAD/Myc-His A, expressed in TOP10 cells with L-arabinose as expression inducer, followed by protein purification by using immobilized metal affinity chromatography (IMAC). The optimal expression condition was determined by incubation with 0.02% of L-arabinose for 4 hours at 37°C. A total of 2 mg/ml of purified scygonadin with the molecular weight of ~17kDa was succesfully obtained. The results demonstrated that the recombinant scygonadin was successfully produced in heterologous expression system which may allow production of scygonadin in large quantities for further research and commercial application.
format	Article
author	Nurfarhana Rosli, Farah Ayunie Mohd Zain, Sandra Catherine Zainathan, Siti Nor Khadijah Addis,
spellingShingle	Nurfarhana Rosli, Farah Ayunie Mohd Zain, Sandra Catherine Zainathan, Siti Nor Khadijah Addis, Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata
author_facet	Nurfarhana Rosli, Farah Ayunie Mohd Zain, Sandra Catherine Zainathan, Siti Nor Khadijah Addis,
author_sort	Nurfarhana Rosli,
title	Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata
title_short	Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata
title_full	Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata
title_fullStr	Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata
title_full_unstemmed	Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata
title_sort	heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab scylla serrata
publisher	Penerbit Universiti Kebangsaan Malaysia
publishDate	2019
url	http://journalarticle.ukm.my/12781/ http://journalarticle.ukm.my/12781/ http://journalarticle.ukm.my/12781/1/48_01_14.pdf
first_indexed	2023-09-18T20:03:22Z
last_indexed	2023-09-18T20:03:22Z
_version_	1777406996595605504

Heterologous expression of recombinant scygonadin antimicrobial peptide from mud crab Scylla serrata

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