A saposin domain-containing protein of tongue sole Cynoglossus semilaevis: Antimicrobial activity and mechanism

Prosaposin is a precursor that can be processed into four different saposins, designated as A, B, C, and D, which have multiple functions in mammals, including neuroprotection and immune modulation. The immune function of saposin in teleost remains largely unknown. In the present study, a saposin (S...

Full description

Saved in:
Bibliographic Details
Published in:Developmental and comparative immunology 2023-04, Vol.141, p.104633-104633, Article 104633
Main Authors: Tong, Jiazhou, Guan, Xiaolu, Jiang, Shuai, Sun, Li
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Anti-Infective Agents
Anti-microbial activity
Cynoglossus semilaevis
Fish Diseases
Fish Proteins
Flatfishes
HEK293 Cells
Humans
Immunity
Mammals
Saposin domain-containing protein
Saposins - genetics
Saposins - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Prosaposin is a precursor that can be processed into four different saposins, designated as A, B, C, and D, which have multiple functions in mammals, including neuroprotection and immune modulation. The immune function of saposin in teleost remains largely unknown. In the present study, a saposin (SAP) domain-containing protein was identified in half-smooth tongue sole Cynoglossus semilaevis and named CsSDP. CsSDP harbors one SAP A domain and two SAP B domains. When expressed in HEK293T cells, CsSDP was specifically localized in the lysosome. When overexpressed in Escherichia coli, CsSDP markedly inhibited bacterial growth, and the inhibitory effect depended on two specific regions in the SAP A and SAP B domains. Two polypeptides (P32 and P30) derived from the above SAP A and B domains could bind to and inhibit the growth of both Gram-negative and Gram-positive bacteria. The ultrastructural analysis revealed that P32 and P30 killed target bacteria by disrupting the bacterial cell wall and inducing substantial release of cytoplasmic contents. These results shed new lights on the immune function of saposin domain-containing protein in teleost. •CsSDP exhibits unique structural feature with robust antimicrobial activity.•P30 and P32 derived from CsSDP functioned as antimicrobial peptides.•P30 and P32 killed target bacteria by disruption of the bacterial cell wall.
ISSN:0145-305X
1879-0089
DOI:10.1016/j.dci.2023.104633