Journal
FISH & SHELLFISH IMMUNOLOGY
Volume 80, Issue -, Pages 274-280Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fsi.2018.06.019
Keywords
Ruditapes philippinarum; Defensin; Antimicrobial activity; Membrane disruption
Funding
- National Natural Science Foundation of China [41476126]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDA11020305]
- Key Research Program of the Chinese Academy of Sciences [KZZD-EW-14]
- Youth Innovation Promotion Association CAS [2016196]
Ask authors/readers for more resources
Defensins are small cysteine-rich cationic proteins that are ubiquitously present in both vertebrates and invertebrates and constitute the front line of host innate immunity. In the present study, a defensin-like antimicrobial peptide (designed as RpdefB) was identified and characterized from the manila clam Ruditapes philippinarum. The open reading frame of RpdefB encoded a 70-amino acid polypeptide with a calculated molecular mass of 7.5 kDa and isoelectric point of 8.16. Multiple alignments and phylogenetic analysis strongly suggested that RpdefB was a new member of the defensin family. In non-stimulated clams, RpdefB transcripts were constitutively expressed in all five tested tissues, especially in the hepatopancreas. After Vibrio anguillarum challenge, expression of RpdefB mRNA in hemocytes was significantly up-regulated at 6h, 12 h and 72 h. The synthetic peptide RpdefB showed high antibacterial activity against the Gram-negative bacterium Vibrio splendidus. Moreover, membrane integrity analysis revealed that RpdefB increased the membrane permeability of Escherichia coli and then resulted in cell death. Overall, our results suggested that RpdefB played an important role in the elimination of invading bacterium, perhaps through membrane-disruptive activity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available