This study provides new insights about the epidemiology of CMV-GBS and shows that the risk of developing GBS is similar following primary CMV infection or C. jejuni infection. Our results also suggest a direct or indirect involvement of viral replication in the neuropathological processes of CMV-GBS.

We studied 315 coagulase-negative Staphylococcus strains recovered prospectively during 240 surgical procedures (206 subjects) from proven or suspected device-associated bone and joint infections. Sixteen strains (5.1%) had decreased susceptibility to glycopeptides: 15 (12 S. epidermidis strains, 2 S. capitis strains, and 1 S. haemolyticus strain) to teicoplanin alone (MIC of 16 mg/liter, n ‫؍‬ 9; MIC of 32 mg/liter, n ‫؍‬ 6) and one (S. epidermidis) to both teicoplanin and vancomycin (MIC, 16 and 8 mg/liter, respectively). Decreased susceptibility to teicoplanin was more prevalent in "infecting" strains (i.e., strains recovered from >2 distinct intraoperative samples) than in "contaminants"

Glycopeptides and ␤-lactams are the major antibiotics available for the treatment of infections due to Gram-positive bacteria. Emergence of cross-resistance to these drugs by a single mechanism has been considered as unlikely because they inhibit peptidoglycan polymerization by different mechanisms. Therapeutic usage of antibiotics has invariably led to emergence of resistance in target pathogens and members of commensal flora submitted to the same selective pressure. This scenario differs greatly between antibiotics with respect to the time period separating initial drug marketing and emergence of resistance (1). Detoxification of penicillin was recognized before the first therapeutic usage of the drug (2), and acquisition of resistance was immediately a medical concern (3). In contrast, acquired resistance to glycopeptides was detected for the first time in enterococci 28 years after vancomycin had been launched in 1956 (4). During this unusually long delay, glycopeptides were considered as "irresistible" antibiotics, and it has been rationalized that this class of drugs remained unharmed because of its unique mode of action (5). The drugs bind to the peptidyl-D-Ala 4 -D-Ala 5 extremity of peptidoglycan precursors at the bacterial cell surface and block the transglycosylation and transpeptidation reactions by steric hindrance (Fig. 1A). This mode of action implies that acquisition of resistance cannot be easily achieved because modification of the target is limited by the specificity of multiple biosynthetic enzymes (5), including the Ddl ligase for synthesis of D-Ala-D-Ala, the MurF ligase for addition of the resulting dipeptide to the nascent cytoplasmic precursor, and the D,D-transpeptidases for peptidoglycan crosslinking in the last step of peptidoglycan polymerization (6). The latter reaction is catalyzed by penicillin-binding proteins (PBPs) 2 that cleave the D-Ala 4 -D-Ala 5 bond of a donor stem pentapeptide and link the carboxyl of D-Ala 4 to the amino group of the side chain carried by the third residue of an acceptor stem peptide (Fig. 1A).Glycopeptide resistance has emerged in the enterococci (4) by acquisition of transposon Tn1546, which mediates production of precursors terminating in D-lactate (D-Lac) instead of D-Ala (7,8). The substitution leads to a 1,000-fold reduction in the affinity of vancomycin for its target (9).