A histone H2A-derived antimicrobial peptide, Hipposin from mangrove whip ray,Himantura walga: Molecular and functional characterisation
A histone H2A-derived antimicrobial peptide, Hipposin from mangrove whip ray,Himantura walga: Molecular and functional characterisation
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DOI：
10.1007/s13205-020-02455-3
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发表时间：
2020-10-09
期刊：
影响因子：
2.8
通讯作者：
Rosamma, Philip
中科院分区：
文献类型：
--
作者：
Athira, P. P.;Anju, M. V.;Rosamma, Philip
抗菌肽（Antimicrobial peptides，AMP）是由所有类型的生物体产生的生物动态分子，作为其先天免疫系统的基本组成部分。从红树林鞭鳐（Himantura walga）中分离鉴定了一种组蛋白H2 A抗菌肽Hipposin。从互补DNA中扩增出编码81个氨基酸残基的243 bp片段，经鉴定为Hipposin，命名为Hw-Hip。同源性分析表明，Hw-Hip属于组蛋白H2 A超家族，与其它鱼类组蛋白AMP具有同源性。Hw-Hip的系统发育分析显示与鱼类H2 A组蛋白聚类。二级结构分析表明，存在三个α-螺旋和四个无规卷曲与一个突出的脯氨酸铰链。Hw-Hip的理化性质与抗菌肽的性质一致。39-mer活性肽序列通过计算机蛋白水解切割释放。活性肽的功能表征在计算机上显示抗菌，抗癌和抗肿瘤膜活性，使Hw-Hip有希望的候选人进行进一步的探索。
Antimicrobial peptides (AMPs) are biologically dynamic molecules produced by all type of organisms as a fundamental component of their innate immune system. The present study deals with the identification of a histone H2A-derived antimicrobial peptide, Hipposin from mangrove whip ray,Himantura walga. A 243 base pair fragment encoding 81 amino acid residues amplified from complementary DNA was identified as Hipposin and termed asHw-Hip. Homologous analysis showed thatHw-Hip belongs to the Histone H2A superfamily and shares sequence identity with other histone-derived AMPs from fishes. Phylogenetic analysis ofHw-Hip displayed clustering with the fish H2A histones. Secondary structure analysis showed the presence of three alpha-helices and four random coils with a prominent proline hinge. The physicochemical properties ofHw-Hip are in agreement with the properties of antimicrobial peptides. A 39-mer active peptide sequence was released by proteolytic cleavage in silico. Functional characterisation of active peptide in silico revealed antibacterial, anticancer and antibiofilm activities makingHw-Hip a promising candidate for further exploration.