[Hospital readmission induced by adverse drug reaction: a pilot study in a post-emergency unit of a French university hospital].

Purpose: Adverse Drug Reactions (ADRs) leading to hospital admission was estimated to 3.6 to 21.7%.

Human T- and B-cell epitopes of E1 glycoprotein of rubella virus.

The identification of T- and B-cell sites recognized frequently by human populations could provide the basis for selecting the candidate T- and B-cell epitopes for the development of an effective synthetic vaccine against rubella. Rubella virus E1 glycoprotein has been shown to be the predominant antigen to which the majority of human populations develop lymphocyte proliferative and antibody responses. To define the T- and B-cell epitopes of E1 glycoprotein of rubella virus, 23 overlapping synthetic peptides corresponding to more than 90% of the amino acid sequence of E1 were synthesized and tested for their capacities to induce proliferative and antibody responses of 10 seropositive individuals.

Cellular and humoral immune responses to rubella virus structural proteins E1, E2, and C.

Better understanding of cell-mediated immune responses to rubella virus would provide the basis for the development of safe and effective vaccines against rubella and would aid in analysis of the pathophysiology of congenital rubella syndrome. We have expressed individual rubella virus structural proteins, E1, E2 and C, via vaccinia virus recombinants. Using the expressed recombinant proteins as antigens, we were able to demonstrate antigen-specific lymphocyte proliferative responses in control individuals and individuals with congenital rubella syndrome.

Localization of the virus neutralizing and hemagglutinin epitopes of E1 glycoprotein of rubella virus.

Current serological assays using whole rubella virus (RV) as a target antigen for detecting RV-specific antibodies fail to define specific RV proteins and antigenic determinants such as hemagglutinin (HA) and virus-neutralizing (VN) epitopes of rubella virus. A panel of E1 deletion mutants and a subset of E1-specific monoclonal antibodies (MAb) were used for the initial analysis of HA and VN epitopes of E1 glycoprotein. A peptide region (E1(193) to E1(269)) was found to contain HA and VN epitopes.

Analysis of rubella virus E1 glycosylation mutants expressed in COS cells.

cDNA clones encoding the envelope glycoprotein E1 of rubella virus (RV) were altered by site-directed mutagenesis at consensus sites for addition of N-linked glycans. The resulting plasmids were introduced into COS cells and the mutant E1 proteins were analyzed by indirect immunofluorescence, radioimmunoprecipitation, and immunoblotting. We found that RV E1 contains three N-linked oligosaccharides, each approximately 2 kDa in size.