Study of the interactions between endolysin and bacterial peptidoglycan on S. aureus by dynamic force spectroscopy

Nanoscale ◽  
2015 ◽  
Vol 7 (37) ◽  
pp. 15245-15250 ◽  
Author(s):  
Jianli Liu ◽  
Xuejie Zhang ◽  
Hang Yang ◽  
Jinghe Yuan ◽  
Hongping Wei ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacterial Pathogen ◽  
Force Spectroscopy ◽  
Binding Domain ◽  
Dynamic Force ◽  
Dynamic Force Spectroscopy ◽  
Binding Strength ◽  
Cell Wall Binding ◽  
Cell Wall Binding Domain ◽  
Bacterial Peptidoglycan

The cell wall binding domain (CBD) of bacteriophage lysins can bind to host bacteria with comparable binding strength as antibody, demonstrating it is a promising new probe to detect the corresponding bacterial pathogen.

scholarly journals LysPBC2, a Novel Endolysin Harboring aBacillus cereusSpore Binding Domain

2018 ◽  
Vol 85 (5) ◽  
Author(s):  
Minsuk Kong ◽  
Hongjun Na ◽  
Nam-Chul Ha ◽  
Sangryeol Ryu
Keyword(s):  
Cell Wall ◽  
Catalytic Domain ◽  
Binding Activity ◽  
Binding Domain ◽  
Lytic Activity ◽  
Content Type ◽  
Cell Wall Binding ◽  
A Cell ◽  
Cell Wall Binding Domain

ABSTRACTTo control the spore-forming human pathogenBacillus cereus, we isolated and characterized a novel endolysin, LysPBC2, from a newly isolatedB. cereusphage, PBC2. Compared to the narrow host range of phage PBC2, LysPBC2 showed very broad lytic activity against allBacillus,Listeria, andClostridiumspecies tested. In addition to a catalytic domain and a cell wall binding domain, LysPBC2 has a spore binding domain (SBD) partially overlapping its catalytic domain, which specifically binds toB. cereusspores but not to vegetative cells ofB. cereus. Both immunogold electron microscopy and a binding assay indicated that the SBD binds the external region of the spore cortex layer. Several amino acid residues required for catalytic or spore binding activity of LysPBC2 were determined by mutagenesis studies. Interestingly, LysPBC2 derivatives with impaired spore binding activity showed an increased lytic activity against vegetative cells ofB. cereuscompared with that of wild-type LysPBC2. Further biochemical studies revealed that these LysPBC2 derivatives have lower thermal stability, suggesting a stabilizing role of SBD in LysPBC2 structure.IMPORTANCEBacteriophages produce highly evolved lytic enzymes, called endolysins, to lyse peptidoglycan and release their progeny from bacterial cells. Due to their potent lytic activity and specificity, the use of endolysins has gained increasing attention as a natural alternative to antibiotics. Since most endolysins from Gram-positive-bacterium-infecting phages have a modular structure, understanding the function of each domain is crucial to make effective endolysin-based therapeutics. Here, we report the functional and biochemical characterization of aBacillus cereusphage endolysin, LysPBC2, which has an unusual spore binding domain and a cell wall binding domain. A single point mutation in the spore binding domain greatly enhanced the lytic activity of endolysin at the cost of reduced thermostability. This work contributes to the understanding of the role of each domain in LysPBC2 and will provide insight for the rational design of efficient antimicrobials or diagnostic tools for controllingB. cereus.

scholarly journals Mur1, aStreptococcus thermophiluspeptidoglycan hydrolase devoid of a specific cell wall binding domain

2000 ◽  
Vol 187 (1) ◽  
pp. 69-76 ◽  
Author(s):  
Clara Husson-Kao ◽  
Jérôme Mengaud ◽  
Laurent Benbadis ◽  
Marie-Pierre Chapot-Chartier
Keyword(s):  
Cell Wall ◽  
Binding Domain ◽  
Specific Cell ◽  
Cell Wall Binding ◽  
Cell Wall Binding Domain

Selective Killing of Pathogenic Bacteria by Antimicrobial Silver Nanoparticle—Cell Wall Binding Domain Conjugates

2018 ◽  
Vol 10 (16) ◽  
pp. 13317-13324 ◽  
Author(s):  
Domyoung Kim ◽  
Seok-Joon Kwon ◽  
Xia Wu ◽  
Jessica Sauve ◽  
Inseon Lee ◽  
...  
Keyword(s):  
Cell Wall ◽  
Silver Nanoparticle ◽  
Pathogenic Bacteria ◽  
Binding Domain ◽  
Cell Wall Binding ◽  
Cell Wall Binding Domain

scholarly journals Endolysin of bacteriophage BFK20: evidence of a catalytic and a cell wall binding domain

2011 ◽  
Vol 321 (2) ◽  
pp. 83-91 ◽  
Author(s):  
Martina Gerova ◽  
Nora Halgasova ◽  
Jana Ugorcakova ◽  
Gabriela Bukovska
Keyword(s):  
Cell Wall ◽  
Binding Domain ◽  
Cell Wall Binding ◽  
A Cell ◽  
Cell Wall Binding Domain
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