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A Non-Canonical Teleost NK-Lysin: Antimicrobial Activity via Multiple Mechanisms
Xu, Hang1,2,3,4; Yuan, Zihao1,2,3; Sun, Li1,2,3,4
2022-11-01
Source PublicationINTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume23Issue:21Pages:15
Corresponding AuthorSun, Li(lsun@qdio.ac.cn)
AbstractNK-lysin (NKL) is a family of antimicrobial proteins with an important role in innate and adaptive immunity. In this study, a non-canonical NK-lysin (NKLnc) was identified in the Japanese flounder (Paralichthys olivaceus), which shares low sequence identities (15.8-20.6%) with previously reported fish NKLs and was phylogenetically separated from the canonical NKLs in teleost. NKLnc expression was upregulated in flounder tissues during bacterial infection, and interference with NKLnc expression impaired the ability of flounder cells to eliminate invading bacteria. When expressed in Escherichia coli, NKLnc was detrimental to the host cells. P35, a peptide derived from the saposin B domain (SapB) of NKLnc, bound major bacterial surface molecules and killed both Gram-negative and Gram-positive bacteria by inflicting damage to bacterial cell structure and genomic DNA. The bactericidal activity, but not the bacteria-binding capacity, of P35 required the structural integrity of the alpha 2/3 helices in SapB. Furthermore, P35 induced the migration of flounder peripheral blood leukocytes, inhibited bacterial dissemination in fish tissues, and facilitated fish survival after bacterial challenge. Together our study reveals that NKLnc plays an important part in flounder immune defense, and that NKLnc peptide exerts an antimicrobial effect via multiple mechanisms by targeting both bacteria and fish cells.
KeywordNK-lysin Paralichthys olivaceus antimicrobial peptide bactericidal
DOI10.3390/ijms232112722
Indexed BySCI
Language英语
Funding ProjectNational Key Research and Development Project of China[2018YFD0900500] ; Taishan Scholar Program of Shandong Province
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Multidisciplinary
WOS IDWOS:000881196400001
PublisherMDPI
Citation statistics
Cited Times:7[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/180417
Collection实验海洋生物学重点实验室
Corresponding AuthorSun, Li
Affiliation1.Chinese Acad Sci, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Ctr Ocean Megasci, Inst Oceanol, Shandong Prov Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
3.Pilot Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266237, Peoples R China
4.Univ Chinese Acad Sci, Coll Earth & Planetary Sci, Beijing 100049, Peoples R China
First Author AffilicationCenter for Ocean Mega-Science, Chinese Academy of Sciences
Corresponding Author AffilicationCenter for Ocean Mega-Science, Chinese Academy of Sciences
Recommended Citation
GB/T 7714
Xu, Hang,Yuan, Zihao,Sun, Li. A Non-Canonical Teleost NK-Lysin: Antimicrobial Activity via Multiple Mechanisms[J]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,2022,23(21):15.
APA Xu, Hang,Yuan, Zihao,&Sun, Li.(2022).A Non-Canonical Teleost NK-Lysin: Antimicrobial Activity via Multiple Mechanisms.INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,23(21),15.
MLA Xu, Hang,et al."A Non-Canonical Teleost NK-Lysin: Antimicrobial Activity via Multiple Mechanisms".INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 23.21(2022):15.
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