Surveillance and endemic vancomycin-resistant enterococci: some success in control is possible.

Vancomycin-resistant enterococci (VRE) are prevalent in many Irish hospitals. We analysed surveillance data from 2001 to 2008 in a centre where VRE is endemic. All clinically significant enterococci were tested for susceptibility to vancomycin. All intensive care unit admissions were screened on admission and weekly thereafter. Interventions included isolating/cohorting VRE patients, monthly prevalence surveys of VRE patients, the introduction of an electronic alert system, programmes to improve hand and environmental hygiene, and the appointment of an antibiotic pharmacist. There was a significant increase in the number of positive VRE screening samples from 2001 (1.96 patients with positive VRE screens per 10 000 bed-days) to 2006 (4.98 per 10 000 bed-days) (P < or = 0.001) with a decrease in 2007 (3.18 per 10 000 bed-days) (P < or = 0.01). The number of VRE bloodstream infections (BSI) increased from 0.09 BSI per 10 000 bed-days in 2001 to 0.78 per 10 000 bed-days in 2005 (P < or = 0.001) but decreased subsequently. Linear regression analysis indicated a significant association between new cases of VRE and non-isolated VRE patients, especially between May 2005 and December 2006 [P=0.009; 95% confidence interval (CI): 0.08-0.46] and between May 2005 and December 2008 (P = 0.008; 95% CI: 0.06-0.46). Routine surveillance for VRE together with other measures can control VRE BSI and colonisation, even where VRE is endemic, and where facilities are constrained.

The protein sequence of an archaeal catalase-peroxidase.

The gene encoding a catalase-peroxidase of archaeal origin, the halophilic catalase-peroxidase from Haloarcula marismortui, was sequenced. The primary structure proposed was confirmed by Edman degradation and mass spectrometry analyses of proteolytic fragments of the purified protein. The open reading frame in the gene corresponds to 731 amino acids and the calculated mass of the mature protein (deleted of the N-terminal methionine) is 81,253.65 Da, in reasonable agreement with the value of 81,292 +/- 9 Da previously measured by mass spectrometry. Southern and Northern blot analyses showed that the protein is encoded by a single gene as a monocistronic transcript. The protein sequence shows a high level of identity with bacterial catalase-peroxidases, with strongly conserved regions around the heme binding histidines. Similarly to other soluble halophilic proteins, it shows the excess of acidic residues that has been associated with solvation in halophilic adaptation.