Endolysin of bacteriophage BFK20: evidence of a catalytic and a cell wall binding domain.
FEMS Microbiol Lett
; 321(2): 83-91, 2011 Aug.
Article
em En
| MEDLINE
| ID: mdl-21592196
ABSTRACT
A gene product of ORF24' was identified on the genome of corynephage BFK20 as a putative phage endolysin. The protein of endolysin BFK20 (gp24') has a modular structure consisting of an N-terminal amidase_2 domain (gp24CD) and a C-terminal cell wall binding domain (gp24BD). The C-terminal domain is unrelated to any of the known cell wall binding domains of phage endolysins. The whole endolysin gene and the sequences of its N-terminal and C-terminal domains were cloned; proteins were expressed in Escherichia coli and purified to homogeneity. The lytic activities of endolysin and its catalytic domain were demonstrated on corynebacteria and bacillus substrates. The binding activity of cell wall binding domain alone and in fusion with green fluorescent protein (gp24BD-GFP) were shown by specific binding assays to the cell surface of BFK20 host Brevibacterium flavum CCM 251 as well as those of other corynebacteria.
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Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Bacteriófagos
/
Proteínas Virais
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article