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2017 ; 7
(ä): 290
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A Novel Chimeric Endolysin with Antibacterial Activity against
Methicillin-Resistant Staphylococcus aureus
#MMPMID28713777
Haddad Kashani H
; Fahimi H
; Dasteh Goli Y
; Moniri R
Front Cell Infect Microbiol
2017[]; 7
(ä): 290
PMID28713777
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Cysteine/histidine-dependent amidohydrolase/peptidase (CHAP) and amidase are
known as catalytic domains of the bacteriophage-derived endolysin LysK and were
previously reported to show lytic activity against methicillin-resistant
Staphylococcus aureus (MRSA). In the current study, the in silico design and
analysis of chimeric CHAP-amidase model was applied to enhance the stability and
solubility of protein, which was achieved through improving the properties of
primary, secondary and tertiary structures. The coding gene sequence of the
chimeric CHAP-amidase was synthesized and subcloned into the pET-22(+) expression
vector, and the recombinant protein was expressed in E. coli BL21 (DE3) strain.
Subsequent affinity-based purification yielded ~12 mg soluble protein per liter
of E. coli culture. Statistical analysis indicated that concentrations of ?1
?g/mL of the purified protein have significant antibacterial activity against S.
aureus MRSA(252) cells. The engineered chimeric CHAP-amidase exhibited 3.2 log
reduction of MRSA(252) cell counts at the concentration of 10 ?g/mL. A
synergistic interaction between CHAP-amidase and vancomycin was detected by using
checkerboard assay and calculating the fractional inhibitory concentration (FIC)
index. This synergistic effect was shown by 8-fold reduction in the minimum
inhibitory concentration of vancomycin. The chimeric CHAP-amidase displayed
strong antibacterial activity against S. aureus, S. epidermidis, and
enterococcus. However, it did not indicate any significant antibacterial activity
against E. coli and Lactococcus lactis. Taken together, these findings suggest
that our chimeric CHAP-amidase might represent potential to be used for the
development of efficient antibacterial therapies targeting MRSA and certain
Gram-positive bacteria.
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