ABSTRACT
BACKGROUND: Emergency physicians commonly treat skin and soft tissue infections. Community-acquired methicillin-resistant Staphylococcus aureus (CA-MRSA) has become the prominent etiologic agent in these infections. The CA-MRSA is resistant to many antibiotics traditionally used to treat skin and soft tissue infections. STUDY OBJECTIVES: We aim to identify how the increased prevalence of CA-MRSA has changed emergency medicine physician (EMP) prescribing and treatment practices for community-acquired skin and soft tissue infections. METHODS: The EMPs in the United States were surveyed between June and December of 2006. Two cases of skin and soft tissue infection were presented, and questions were asked about management. RESULTS: Two hundred seventy-five surveys were returned. The EMPs used a variety of approaches in the antibiotic treatment of skin and soft tissue infections. Two hundred seven (75.3%) of 275 were board-certified EMPs and were included in the analysis. Commonly used agents for outpatient treatment include trimethoprim/sulfamethoxazole, clindamycin, cephalexin, rifampin, and tetracyclines. For patients requiring admission, 60% of providers would include vancomycin in their treatment regimen. CONCLUSION: Many clinicians have changed their practice patterns to include antibiotics that usually display activity against CA-MRSA. However, cephalexin remains a popular agent used for these infections.
Subject(s)
Anti-Bacterial Agents/therapeutic use , Methicillin-Resistant Staphylococcus aureus , Skin Diseases, Bacterial/drug therapy , Staphylococcal Skin Infections/drug therapy , Adult , Certification , Community-Acquired Infections/diagnosis , Community-Acquired Infections/drug therapy , Emergency Medicine , Health Care Surveys , Humans , Male , Middle Aged , Physicians , Professional Practice , Skin Diseases, Bacterial/diagnosis , Soft Tissue Infections , Staphylococcal Skin Infections/diagnosisABSTRACT
Although helix P4 in the catalytic domain of the RNase P ribozyme is known to coordinate magnesium ions important for activity, distinguishing between direct and indirect roles in catalysis has been difficult. Here, we provide evidence for an indirect role in catalysis by showing that while the universally conserved bulge of helix P4 is positioned 5 nt downstream of the cleavage site, changes in its structure can still purturb active site metal binding. Because changes in helix P4 also appear to alter its position relative to the pre-tRNA cleavage site, these data suggest that P4 contributes to catalytic metal ion binding through substrate positioning.
