Since the exposure of mutans streptococci to xylitol is known to select for xylitol-resistant (XR) natural mutants, the occurrence and long-term survival of such xylitol-resistant strains was evaluated in a cross-sectional sampling of participants of the Ylivieska xylitol study four years after the original two-year experimental period. Paraffin-stimulated whole saliva was first collected, and then plaque was collected and pooled. The salivary and dental plaque mutans streptococci were enumerated after growth on TSY20B agar. The proportion of XR strains was determined by autoradiography with 14C-xylitol. A strong and significant correlation (r = 0.645 and p = 0.005) between the number of mutans streptococci in saliva and in dental plaque was observed in non-consumers of xylitol. Such a correlation totally disappeared (r = 0.098 and p = 0.612) in xylitol-exposed consumers (habitual and former xylitol-consumers). The proportion of the salivary XR mutants (35%) in non-consumers (n = 16) was significantly lower than in the xylitol-exposed consumers (79%) (n = 27), (p = 0.0001) or in former consumers (75%) (n = 13), (p = 0.0008) or in the habitual consumers (83%) (n = 14), (p = 0.004). The proportion of XR mutants in dental plaque was, on the average, much lower than in the corresponding saliva. The proportion of XR in the plaque of xylitol non-consumers was half of that of the xylitol-exposed group, but the difference was not statistically significant.(ABSTRACT TRUNCATED AT 250 WORDS)

A variety of plasma-derived (pd) and recombinant (r) factor VIII (FVIII) concentrates are used to prevent and treat bleeding in severe hemophilia A patients. A significant side effect of FVIII replacement is the development of FVIII neutralizing antibodies (inhibitors) in up to 30% of patients receiving FVIII concentrates. The FVIII protein content (FVIII:Ag) per unit of FVIII:C in FVIII concentrates, and how effectively the FVIII:Ag in FVIII concentrates binds to von Willebrand factor (VWF) may provide information relevant for the survival of FVIII:C in vivo and for estimating the risk for inhibitor development. The FVIII:Ag content of nine r-FVIII and nine pd-FVIII concentrates were quantified in this study using two enzyme-linked immunosorbent assay (ELISA) platforms. The two ELISA platforms were based on the use of a monoclonal anti-(FVIII light chain)-IgG and polyclonal anti-FVIII antibodies as capture antibodies and both ELISAs were equally able to detect > or =0.005 IU of FVIII:Ag. Measured in international units, the r-FVIII concentrates contained significantly higher FVIII:Ag per unit of FVIII:C than the pd-FVIII concentrates. The VWF-binding profiles of the r-FVIII and pd-FVIII concentrates were also determined by gel filtration chromatography. Unlike the plasma-derived products, the r-FVIII concentrates invariably contained a fraction of FVIII:Ag molecules (approximately 20%) which was unable to associate with VWF. Given that VWF regulates both factor VIII proteolysis and survival of FVIII:Ag in vivo, the fraction of FVIII:Ag unable to bind to VWF may have a reduced survival and be more susceptible to proteolytic degradation in vivo. The extent to which the fractions of FVIII:Ag in concentrates able and unable to bind to VWF contribute to inhibitor development in severe FVIII-deficient patients is unknown.

The 3.25 percent HBV DNA positivity rate among the anti-HBc-reactive donations and more particularly the low level of HBV DNA observed in occult donations underline the importance of the use of a sensitive assay to detect HBV DNA in conjunction with other markers. The HBV genetic diversity found in our donor population reflects the province demographics, particularly in the Montreal area where most of the positive donors were from.

With a simple in-house ELISA, 73 blood donors were identified as IgA-deficient. From this number, 34 donors, without detectable anti-IgA in their plasma, were added to our IgA-deficient blood donor panel to maximize the management of our inventory of IgA-deficient frozen blood components.