Streptococcus agalactiae (dans rapport de surveillance des maladies infectieuses 1996)

Report (1997)

Streptococcus agalactiae (dans rapport de surveillance des maladies infectieuses 1998)

Report (1999)

Streptococcus agalactiae (dans rapport de surveillance des maladies infectieuses 1999)

Report (2000)

Streptococcus agalactiae (dans rapport de surveillance des maladies infectieuses 2004)

Report (2005)

Streptococcus agalactiae (dans rapport de surveillance des maladies infectieuses par un réseau de laboratoires de microbilogie 2005 + Tendances épidémiologiques 1983-2004)

in Ducoffre, Geneviève (Ed.) Rapport de surveillance des maladies infectieuses par un réseau de laboratoires de microbiologie 2005 + Tendances épidémiologiques 1983-2004 - IPH/EPI REPORT 2005 (2006)

Streptococcus difficile Is a Nonhemolytic Group B, Type Ib Streptococcus

in International Journal of Systematic Bacteriology (1997), 47(1), 81-5

Whole-cell protein electrophoretic analysis of the type strain of Streptococcus difficile (LMG 15799) revealed that this organism was indistinguishable from Streptococcus agalactiae strains. Although LMG ... [more ▼]

Whole-cell protein electrophoretic analysis of the type strain of Streptococcus difficile (LMG 15799) revealed that this organism was indistinguishable from Streptococcus agalactiae strains. Although LMG 15799'r (T = type strain) was originally described as serologically untypeable, we found that this strain was a group B streptococcus belonging to the capsular polysaccharide antigen type Ib group. The biochemical reactivity of S.difficile, which differed from the biochemical reactivity of typical S. agalactiae strains mainly by being less versatile, is similar to the biochemical reactivity of other group B, type Ib streptococci isolated from poikilothermic animals, such as fish and frogs. [less ▲]

Le streptocoque du groupe B, premiere cause d'infections neonatales graves. Epidemiologie et strategies de prevention

in Revue Médicale de Liège (1999), 54(5), 460-7

As soon as the early 70's, group B streptococci (GBS) became clearly predominant in neonatal infections. There was a dramatic increase in the incidence of GBS neonatal sepsis and meningitis throughout ... [more ▼]

As soon as the early 70's, group B streptococci (GBS) became clearly predominant in neonatal infections. There was a dramatic increase in the incidence of GBS neonatal sepsis and meningitis throughout developed countries and GBS emerged as the leading cause of severe neonatal infections. Most of these infections, associated with high mortality and morbidity, could be prevented by intrapartum chemoprophylaxis given to risk mothers. AAP, ACOG and the CDC issued guidelines for their prevention. Today, in Belgium, there are still no recommendations for the prevention of GBS early-onset infections. [less ▲]

Streptocoques du groupe B: culture et recherche rapide d'antigène

Conference (1999, March 26)

Streptocoques du groupe B: premier agent responsable d'infections néonatales graves. Epidémiologie, facteurs de risque, prévention et technique de dépistage.

Conference (2000, August 30)

Streptomyces Albus G Serine Beta-Lactamase. Probing of the Catalytic Mechanism Via Molecular Modelling of Mutant Enzymes

in Biochemical Journal (1992), 282(Pt 1), 189-195

In previous studies, several amino acids of the active site of class A , β-lactamases have been modified by site-directed mutagenesis. On the basis of the catalytic mechanism proposed for the Streptomyces ... [more ▼]

In previous studies, several amino acids of the active site of class A , β-lactamases have been modified by site-directed mutagenesis. On the basis of the catalytic mechanism proposed for the Streptomyces albus G , β-lactamase [Lamotte- Brasseur, Dive, Dideberg, Charlier, Frere & Ghuysen (1991) Biochem. J. 279, 213-221], the influence that these mutations exert on the hydrogen-bonding network of the active site has been analysed by molecular mechanics. The results satisfactorily explain the effects of the mutations on the kinetic parameters of the enzyme's activity towards a set of substrates. The present study also shows that, upon binding a properly structured ,β-lactam compound, the impaired cavity of a mutant enzyme can readopt a functional hydrogen-bonding-network configuration. [less ▲]