Coagulase-negative staphylococci (CNS) were the first organisms in which ac
quired glycopeptide resistance was recognized. Ever since the early reports
. it has been apparent that resistance to teicoplanin is more common than t
hat to vancomycin and that resistance occurs mostly in species such as Stap
hylococcus haemolyticus and Staphylococcus epidermidis. The minimum inhibit
ory concentrations (MICs) of teicoplanin for CNS usually fall over a wide r
ange, and, especially in some methicillin-resistant isolates of the two abo
ve-mentioned species, they can reach and even exceed the resistance breakpo
int. whereas vancomycin MICs tend to remain more stable over a narrower ran
ge within the limits of susceptibility. CNS strains intermediately suscepti
ble and even resistant not only to teicoplanin but also to vancomycin have,
however, been isolated, most frequently from patients subjected to prolong
ed glycopeptide treatment. Laboratory detection of glycopeptide-resistant C
NS may be problematic, mainly because susceptibility tests, particularly th
ose for teicoplanin, are influenced by various technical factors, and agar
diffusion tests may yield false susceptibility data. In studies with experi
mental glycopeptides, some molecules have exhibited improved in vitro activ
ity compared with teicoplanin and vancomycin, but these encouraging microbi
ological findings have not usually been followed by in vivo trials. Stepwis
e and single-step exposure to teicoplanin and vancomycin has allowed stable
clones for which glycopeptide MICs are increased to be obtained from susce
ptible CNS strains, particularly strains of Staphylococcus haemolyticus and
Staphylococcus epidermidis. In these studies, resistance to teicoplanin wa
s generally easier to obtain than resistance to vancomycin, and the levels
of teicoplanin resistance were higher. Population studies have demonstrated
the usually heterogeneous nature of glycopeptide resistance in CNS. Althou
gh glycopeptide-resistant CNS have been shown to differ in several features
from their glycopeptide-susceptible counterparts, the exact mechanism of s
taphylococcal glycopeptide resistance remains unknown.