The highly conserved central loop of domain V of 23S RNA (nucleotides 2042
to 2628; Escherichia coli numbering) is implicated in peptidyltransferase a
ctivity and represents one of the target sites for macrolide, lincosamide,
and streptogramin B antibiotics. DNA encoding domain V (590 bp) of several
species of Enterococcus was amplified by PCR Twenty enterococcal isolates w
ere tested, including Enterococcus faecium (six isolates), Enterococcus fae
calis, Enterococcus avium, Enterococcus durans, Enterococcus gallinarum, En
terococcus casseliflavus (two isolates of each), and Enterococcus raffinosu
s, Enterococcus mundtii, Enterococcus malodoratus, and Enterococcus hirae t
one isolate of each). For all isolates, species identification by biochemic
al testing was corroborated by 16S rRNA gene sequencing, The sequence of do
main V of the 23S rRNA gene from E, faecium and E, faecalis differed from t
hose of all other enterococci, The domain V sequences of E, durans and E, h
irae were identical. This was also true for E, gallinarum and E, casselifla
vus, E, avium differed from E, casseliflavus by 23 bases, from E, durans by
16 bases, and from E, malodoratus by 2 bases. E, avium differed from E, ra
ffinosus by one base. Despite the fact that domain V is considered to be hi
ghly conserved, substantial differences were identified between several ent
erococcal species.