Evaluation of Electromagnetic Fields in a Hospital for Safe Use of Electronic Medical Equipment.

Establishment of electromagnetic compatibility is important in use of electronic medical equipment in hospitals. To evaluate the electromagnetic environment, the electric field intensity induced by electromagnetic radiation in broadcasting spectra coming from outside the hospital was measured in a new hospital building before any patients visited the hospital and 6 months after the opening of the hospital. Various incoming radio waves were detected on the upper floors, with no significant difference in measured levels before and after opening of the hospital. There were no cellphone terminal signals before the hospital opened, but these signals were strongly detected at 6 months thereafter. Cellphone base stations signals were strongly detected on the upper floors, but there were no signals at most locations in the basement and in the center of the building on the lower floors. A maximum electrical intensity of 0.28 V/m from cellphone base stations (2.1 GHz) was detected at the south end of the 2nd floor before the hospital opened. This value is lower than the EMC marginal value for general electronic medical equipment specified in IEC 60601-1-2 (3 V/m). Therefore, electromagnetic interference with electronic medical equipment is unlikely in this situation. However, cellphone terminal signals were frequently detected in non-base station signal areas. This is a concern, and understanding signal strength from cellphone base stations at a hospital is important for promotion of greater safety.

Molecular characterization of a novel beta1,3-galactosyltransferase for capsular polysaccharide synthesis by Streptococcus agalactiae type Ib.

A group B streptococcus, Streptococcus agalactiae type Ib, produces a high-molecular-weight polysaccharide consisting of the following pentasaccharide repeating unit: -->4)-[alpha-D-NeupNAc-(2-->3)-beta-D-Galp-(1-->3)-beta-D-GlcpNAc-(1-->3)]-beta-D-Galp-(1-->4)-beta-D-Glcp-(1-->. The type-specific capsular polysaccharide (CP) synthesis (cps) genes of this strain were cloned and analyzed. A cloned 10-kb DNA fragment contained cpsIbE to L and neu (neuraminic acid synthesis gene) B. Comparison of the gene products with those of S. agalactiae type Ia, which has a similar but distinct CP, showed that the translation products of cpsIa and cpsIb genes exhibited very high homology except for those of cpsJ and K. In the type Ia strain, cpsIaJ encodes beta1,4-galactosyltransferase, which catalyzes the transfer of galactose as the fourth monosaccharide of the sugar repeating unit. In the type Ib CP, this galactose forms a beta1,3-linkage to GlcNAc. The low homology between the type Ia and Ib CpsJs seems to reflect this difference. By enzymatic activity measurement, the cpsIbJ product was found to display beta1,3-galactosyltransferase activity. Furthermore, hydrophobic cluster analysis clarified the similarities and differences of the structures in N-terminal regions, including the DXD motif, between the galactosyltransferases.

Identification of sialyltransferases of Streptococcus agalactiae.

Group B streptococci, Streptococcus agalactiae, produce high-molecular-weight polysaccharides containing N-acetylneuraminic acid. Although the type-specific capsular polysaccharide (CP) synthesis (cps) genes of several S. agalactiae strains have been extensively analyzed, to date, no sialyltransferase activity has been detected from any gene product of the cps gene cluster. Among the cps genes, the cpsK gene products of S. agalactiae types la and Ib showed weak similarity to several bacterial sialyltransferases. In this study, the cpsIaK and cpsIbK gene products were found to show sialyltransferase activity specific for lacto-N-neotetraose and lacto-N-tetraose, respectively. This acceptor specificity seems to reflect the respective CP structure, since the repeating unit of type la CP is sialyllacto-N-neotetraose and that of type Ib CP is sialyllacto-Ntetraose. We also found that the C-terminal regions of CpsKs were almost completely conserved in various S. agalactiae strains.