A macin identified from Venerupis philippinarum: Investigation on antibacterial activities and action mode

Dinglong Yang; Yijing Han; Lizhu Chen; Ruiwen Cao; Qing Wang; Zhijun Dong; Hui Liu; Xiaoli Zhang; Qianqian Zhang; Jianmin Zhao

doi:10.1016/j.fsi.2019.07.031

A macin identified from Venerupis philippinarum: Investigation on antibacterial activities and action mode

Fish Shellfish Immunol. 2019 Sep:92:897-904. doi: 10.1016/j.fsi.2019.07.031. Epub 2019 Jul 11.

Authors

Affiliations

¹ Muping Coastal Environment Research Station, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai, 264003, PR China; Research and Development Center for Efficient Utilization of Coastal Bioresources, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai, 264003, PR China.
² Muping Coastal Environment Research Station, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai, 264003, PR China; University of Chinese Academy of Sciences, Beijing, 100049, PR China.
³ Shandong Marine Resource and Environment Research Institute, Yantai, 264006, PR China.
⁴ Muping Coastal Environment Research Station, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai, 264003, PR China; Research and Development Center for Efficient Utilization of Coastal Bioresources, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai, 264003, PR China; Center for Ocean Mega-science, Chinese Academy of Sciences, Qingdao, Shandong, 266071, PR China. Electronic address: jmzhao@yic.ac.cn.

PMID: 31302284
DOI: 10.1016/j.fsi.2019.07.031

Abstract

In the present study, a macin was cloned and characterized from clam Venerupis philippinarum (designed as VpMacin). The full-length cDNA of VpMacin was of 579 bp, encoding a peptide of 87 amino acids with the predicted molecular weight of 9.7 kDa. Analysis of the conserved domain suggested that VpMacin was a new member of the macin family. In non-stimulated clams, VpMacin transcripts exhibited different tissue expression pattern, and highly expressed in the tissues of gills and hepatopancreas. Generally, the temporal expression of VpMacin transcripts was significantly induced in hemocytes of clams post Vibrio anguillarum challenge. Moreover, the recombinant VpMacin protein (rVpMacin) showed obvious antimicrobial activities against Gram-positive and Gram-negative bacteria. After incubated with 40 μM rVpMacin, all detected Escherichia coli could be killed within 60 min. Membrane integrity analysis revealed that rVpMacin could increase the membrane permeability of bacteria and then resulted in cell death. Overall, our results suggested that VpMacin had an important function in host defense against invasive pathogens.

Keywords: Antimicrobial activity; Macin; Molecular characterization; Venerupis philippinarum.

MeSH terms

Amino Acid Sequence
Animals
Anti-Bacterial Agents / pharmacology
Antimicrobial Cationic Peptides / chemistry
Antimicrobial Cationic Peptides / genetics*
Antimicrobial Cationic Peptides / immunology*
Bivalvia / genetics*
Bivalvia / immunology*
Bivalvia / microbiology
Gram-Negative Bacteria / physiology*
Gram-Positive Bacteria / physiology*
Sequence Alignment
Transcriptome

Substances

Anti-Bacterial Agents
Antimicrobial Cationic Peptides