Journal Article
	
	
				- Characterization of staphylococcal endolysin LysSAP33 possessing untypical domain composition
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		Jun-Hyeok Yu , Do-Won Park , Jeong-A Lim , Jong-Hyun Park 		
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			J. Microbiol. 2021;59(9):840-847.   Published online August 12, 2021		
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							DOI: https://doi.org/10.1007/s12275-021-1242-1
					
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						 Abstract Abstract PDF PDF
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		Endolysin, a peptidoglycan hydrolase derived from bacteriophage,
has been suggested as an alternative antimicrobial
agent. Many endolysins on staphylococcal phages have been
identified and applied extensively against Staphylococcus spp.
Among them, LysK-like endolysin, a well-studied staphylococcal
endolysin, accounts for most of the identified endolysins.
However, relatively little interest has been paid to LysKunlike
endolysin and a few of them has been characterized.
An endolysin LysSAP33 encoded on bacteriophage SAP33
shared low homology with LysK-like endolysin in sequence
by 41% and domain composition (CHAP-unknown CBD).
A green fluorescence assay using a fusion protein for Lys-
SAP33_CBD indicated that the CBD domain (157-251 aa)
was bound to the peptidoglycan of S. aureus. The deletion of
LysSAP33_CBD at the C-terminal region resulted in a significant
decrease in lytic activity and efficacy. Compared to
LysK-like endolysin, LysSAP33 retained its lytic activity in a
broader range of temperature, pH, and NaCl concentrations.
In addition, it showed a higher activity against biofilms than
LysK-like endolysin. This study could be a helpful tool to develop
our understanding of staphylococcal endolysins not
belonging to LysK-like endolysins and a potential biocontrol
agent against biofilms.	
		
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			Citations Citations to this article as recorded by    
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 Mina Golban, Javad Charostad, Hossein Kazemian, Hamid Heidari
 Infectious Diseases and Therapy.2025; 14(1): 13.     CrossRef
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 Research Support, Non-U.S. Gov't
	
	
				- Fatty Acid Biosynthesis in Eukaryotic Photosynthetic Microalgae: Identification of a Microsomal Delta 12 Desaturase in Chlamydomonas reinhardtii
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		Xiaoyuan Chi , Xiaowen Zhang , Xiangyu Guan , Ling Ding , Youxun Li , Mingqing Wang , Hanzhi Lin , Song Qin 		
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			J. Microbiol. 2008;46(2):189-201.   Published online June 11, 2008		
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							DOI: https://doi.org/10.1007/s12275-007-0223-3
					
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						 Abstract Abstract PDF PDF
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		Polyunsaturated fatty acids (PUFAs) are important components of infant and adult nutrition because they serve as structural elements of cell membranes. Fatty acid desaturases are responsible for the insertion of double bonds into pre-formed fatty acid chains in reactions that require oxygen and reducing equivalents. In this study, the genome-wide characterization of the fatty acid desaturases from seven eukaryotic photosynthetic microalgae was undertaken according to the conserved histidine-rich motifs and phylogenetic profiles. Analysis of these genomes provided insight into the origin and evolution of the pathway of fatty acid biosynthesis in eukaryotic plants. In addition, the candidate enzyme from Chlamydomonas reinhardtii with the highest similarity to the microsomal Δ12 desaturase of Chlorella vulgaris was isolated, and its function was verified by heterologous expression in yeast (Saccharomyces cerevisiae).	
		
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