BigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity

Penaeidins are members of an antimicrobial peptide (AMP) family that have broad anti-microbial activities only found in penaeid shrimps. The LvBigPEN, a member of penaeidins from shrimp Litopenaeus vannamei, has showed antiviral activity against white spot syndrome virus (WSSV) in our previous repor...

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Autores principales:	Bang Xiao, Xuzheng Liao, Haiyang Wang, Jianguo He, Chaozheng Li
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Antimicrobial peptide Penaeidins V. parahaemolyticus AP-1 pathway Zoology QL1-991
Acceso en línea:	https://doaj.org/article/8dfd2f0d510c48019d24cd99bcea481d
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spelling	oai:doaj.org-article:8dfd2f0d510c48019d24cd99bcea481d2021-11-18T04:53:46ZBigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity2667-011910.1016/j.fsirep.2021.100034https://doaj.org/article/8dfd2f0d510c48019d24cd99bcea481d2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2667011921000293https://doaj.org/toc/2667-0119Penaeidins are members of an antimicrobial peptide (AMP) family that have broad anti-microbial activities only found in penaeid shrimps. The LvBigPEN, a member of penaeidins from shrimp Litopenaeus vannamei, has showed antiviral activity against white spot syndrome virus (WSSV) in our previous report. However, whether LvBigPEN possesses potential anti-bacterial activities is still unknown. Herein, we found that the LvBigPEN played an important role in restricting the infection of Vibrio parahaemolyticus, a natural and Gram-negative bacteria pathogen in shrimp. The transcription of LvBigPEN was strongly induced after V. parahaemolyticus challenge. RNA interference (RNAi) mediated knockdown of LvBigPEN showed that LvBigPEN had a potential antibacterial function against V. parahaemolyticus. Microorganism binding assays indicated that rLvBigPEN could bind to both Gram-negative bacteria and Gram-positive bacteria. Transmission electron microscopy (TEM) analysis showed its ability to destroy bacterial cells in vitro. Besides, in a gel retardation assay, rLvBigPEN could bind to plasmid DNA and bacteria (V. parahaemolyticus) genomic DNA in a concentration-dependent manner. Moreover, the AP-1 pathway could participate in the transcription of LvBigPEN by the dual luciferase reporter assays. Taken together, these results suggested that LvBigPEN possessed the antibacterial activity against V. parahaemolyticus and may be alternative agents for the prevention and treatment of diseases caused by V. parahaemolyticus.Bang XiaoXuzheng LiaoHaiyang WangJianguo HeChaozheng LiElsevierarticleAntimicrobial peptidePenaeidinsV. parahaemolyticusAP-1 pathwayZoologyQL1-991ENFish and Shellfish Immunology Reports, Vol 2, Iss , Pp 100034- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Antimicrobial peptide Penaeidins V. parahaemolyticus AP-1 pathway Zoology QL1-991
spellingShingle	Antimicrobial peptide Penaeidins V. parahaemolyticus AP-1 pathway Zoology QL1-991 Bang Xiao Xuzheng Liao Haiyang Wang Jianguo He Chaozheng Li BigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity
description	Penaeidins are members of an antimicrobial peptide (AMP) family that have broad anti-microbial activities only found in penaeid shrimps. The LvBigPEN, a member of penaeidins from shrimp Litopenaeus vannamei, has showed antiviral activity against white spot syndrome virus (WSSV) in our previous report. However, whether LvBigPEN possesses potential anti-bacterial activities is still unknown. Herein, we found that the LvBigPEN played an important role in restricting the infection of Vibrio parahaemolyticus, a natural and Gram-negative bacteria pathogen in shrimp. The transcription of LvBigPEN was strongly induced after V. parahaemolyticus challenge. RNA interference (RNAi) mediated knockdown of LvBigPEN showed that LvBigPEN had a potential antibacterial function against V. parahaemolyticus. Microorganism binding assays indicated that rLvBigPEN could bind to both Gram-negative bacteria and Gram-positive bacteria. Transmission electron microscopy (TEM) analysis showed its ability to destroy bacterial cells in vitro. Besides, in a gel retardation assay, rLvBigPEN could bind to plasmid DNA and bacteria (V. parahaemolyticus) genomic DNA in a concentration-dependent manner. Moreover, the AP-1 pathway could participate in the transcription of LvBigPEN by the dual luciferase reporter assays. Taken together, these results suggested that LvBigPEN possessed the antibacterial activity against V. parahaemolyticus and may be alternative agents for the prevention and treatment of diseases caused by V. parahaemolyticus.
format	article
author	Bang Xiao Xuzheng Liao Haiyang Wang Jianguo He Chaozheng Li
author_facet	Bang Xiao Xuzheng Liao Haiyang Wang Jianguo He Chaozheng Li
author_sort	Bang Xiao
title	BigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity
title_short	BigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity
title_full	BigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity
title_fullStr	BigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity
title_full_unstemmed	BigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity
title_sort	bigpen, an antimicrobial peptide of penaeidin family from shrimp litopenaeus vannamei with membrane permeable and dna binding activity
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/8dfd2f0d510c48019d24cd99bcea481d
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BigPEN, an antimicrobial peptide of penaeidin family from shrimp Litopenaeus vannamei with membrane permeable and DNA binding activity

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