AUTHOR=Roy Utpal , Chalasani Ajay G. , Shekh M. Raeesh 

TITLE=The anti-Candida activity by Ancillary Proteins of an Enterococcus faecium strain

JOURNAL=Frontiers in Microbiology

VOLUME=6

YEAR=2015

URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2015.00339

DOI=10.3389/fmicb.2015.00339

ISSN=1664-302X

ABSTRACT=<p>An antimycotic activity toward seven strains of <italic>Candida albicans</italic> was demonstrated erstwhile by a wild-type <italic>Enterococcus faecium</italic> isolated from a penguin rookery of the Antarctic region. In the present study the antimicrobial principle was purified by ion exchange and gel permeation chromatography and further was analyzed by LC-ESI-MS/MS. In the purification steps, the dialyzed concentrate and ion exchange fractions inhibited <italic>C. albicans</italic> MTCC 3958, 183, and SC 5314. However, the gel filtration purified fractions inhibited MTCC 3958 and 183. The data obtained from the LC-ESI-MS/MS indicate that the antimicrobial activity of the anti-<italic>Candida</italic> protein produced by <italic>E. faecium</italic> is facilitated by Sag A/Bb for the binding of the indicator organism's cell membrane. Partial N-terminal sequence revealed 12 N-terminal amino acid residues and its analysis shown that it belongs to the LysM motif. The nucleotide sequence of PCR-amplified product could detect 574 nucleotides of the LysM gene responsible for binding to chitin of the cell wall of <italic>Candida</italic> sp.</p>