2018
DOI: 10.1021/acs.jafc.8b02489
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Yeast Surface Display of Antheraea pernyi Lysozyme Revealed α-Helical Antibacterial Peptides in Its N-Terminal Domain

Abstract: The present study investigated a novel lysozyme ApLyz from the Chinese oak silkmoth, Antheraea pernyi, for its active expression with N- or C-terminus fused to the yeast cell surface, and the antimicrobial activities of the corresponding expressed lysozymes were evaluated. The bactericidal activity of C-terminal fusion of ApLyz surpassed that of the N-terminal fusion, which revealed the implication of an N-terminal stretch of ApLyz in the bactericidal function based on the structural mobility of this region. T… Show more

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Cited by 7 publications
(4 citation statements)
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“…A new type of lysozyme from the Chinese oak silk moth ( Antheraea pernyi ) was investigated and the encouraging results obtained about the strong effectiveness against Gram-negative strains, according to the authors, laid the foundation for future improvement by protein engineering [ 64 ].…”
Section: Sourcesmentioning
confidence: 99%
“…A new type of lysozyme from the Chinese oak silk moth ( Antheraea pernyi ) was investigated and the encouraging results obtained about the strong effectiveness against Gram-negative strains, according to the authors, laid the foundation for future improvement by protein engineering [ 64 ].…”
Section: Sourcesmentioning
confidence: 99%
“…ATCC 10988 (GenBank: AAA27695.1) [25]. The mode of fusion has an important effect on the function of the fusion protein, depending mainly on the structure of the protein [26]. To ensure the activity of levansucrase, two yeast display systems, a-agglutinin and Flo1p, were chosen to display levansucrase on the cell surface of S. cerevisiae.…”
Section: Construction Of Two Yeast Cell Surface Display Systemsmentioning
confidence: 99%
“…Use of a yeast surface display platform to anchor recombinant proteins to yeast cell wall has been widely adapted in the biomedical field for antibody and antimicrobial peptide engineering, protein stability, protein–protein interaction, and enzyme metabolic studies ( Cherf and Cochran, 2015 ; Wen et al, 2018 ; Medina-Cucurella et al, 2019 ; Lau et al, 2021 ; Luo et al, 2021 ; Fiebig et al, 2022 ; Kuroda and Ueda, 2022 ; Raeeszadeh-Sarmazdeh and Boder, 2022 ; Teymennet-Ramirez et al, 2022 ). A common yeast display system involves fusing recombinant proteins to the a-agglutinin mating protein Aga2p and expressing extracellularly in yeast that secrete the ß 1,6 glucan-anchored Aga1p domain of a-agglutinin to form an Aga1p–Aga2p complex via two disulfide bonds ( Wang et al, 2005 ; Cherf and Cochran, 2015 ).…”
Section: Introductionmentioning
confidence: 99%