Journal
FISH & SHELLFISH IMMUNOLOGY
Volume 131, Issue -, Pages 77-83Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fsi.2022.09.068
Keywords
Ruditapes philippinarum; Histone; Antimicrobial activity; Extracellular traps
Funding
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDA23050303]
- National Natural Science Foundation of China [41806196, 42176141]
- Youth Innovation Promotion Association, Chinese Academy of Sciences [2022211]
- Natural Science Foundation of Shandong Province [ZR2019BD022]
- Yantai Science and Technology Development Project [2020MSGY066]
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In this study, a novel histone H2A (RpH2A) was identified in clam Ruditapes philippinarum and found to play a crucial role in immune responses by functioning as antimicrobial peptides.
In the present study, a histone H2A (designed as RpH2A) was identified and characterized from clam Ruditapes philippinarum, and its open reading frame (ORF) was of 387 bp encoding a polypeptide of 128 amino acids. The deduced amino acid sequence of RpH2A shared high identities ranging from 57.1% to 96.1% with that of other identified H2A. The mRNA expression of RpH2A was up-regulated significantly after Vibrio anguillarum chal-lenge. The recombinant RpH2A protein (rRpH2A) displayed significantly binding affinity to lipopolysaccharide (LPS) and peptidoglycan (PGN) in vitro, and also exhibited antimicrobial properties against Escherichia coli. In addition, the antimicrobial RpH2A was shown to co-localize with extracellular traps (ETs) released from he-mocytes induced by E. coli, suggesting that RpH2A might contribute to eliminate invading bacteria in clam ETs. Altogether, our data revealed that RpH2A could function as antimicrobial peptides, which might play a crucial role in the immune responses of hemocytes ETs in clams.
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