Dalbavancin (DAL) is a semi-synthetic antibiotic that belongs to the lipoglycopeptide family and is structurally derived from teicoplanin, respect of which it has two structural differences that enhance its anti-staphylococcal binding affinity and extend its half-life to between 149 and 250 hours. It achieves adequate tissue penetration in the skin, bones, joints, lung tissues, and peritoneal space, maintaining concentrations above the MIC for susceptible Gram-positive pathogen. DAL is a bactericidal antimicrobial agent that binds the C-terminal D-alanyl-D-alanine on the bacterial cell wall, blocking trans-glycosylation and transpeptidation processes essential for cell wall synthesis. It seems also to be able to enhance neutrophil antibacterial activity improving PMNs' intracellular killing of MRSA. It has also a good antibiofilm activity, alone or in combination with other molecules. Like other glycopeptide molecules, DAL shares a similar spectrum of activity, with demonstrated in vitro activity against various Gram-positive bacteria, including Staphylococcus spp, Streptococcus spp and Enterococcus (faecium, and faecalis). Resistance to DAL is possible in these gram-positives bacteria, given to presence of enzymes that produce low-affinity binding precursors for the antibiotic's binding site. DAL is capable to overcome Van-B mechanism of resistance, but it results not active in producing Van-A strains. The study objectives was to evaluate efficacy and safety of DAL treatment.