[Self-collected vaginal swabs to diagnosis bacterial vaginosis during pregnancy: A pilot study]. / Autoprélèvement vaginal à la recherche d'une vaginose bactérienne pendant la grossesse: étude pilote.

OBJECTIVE: To study the feasibility of a screening for bacterial vaginosis by a self-collected vaginal swab during pregnancy. To measure bacterial vaginosis prevalence in a non-representative sample of women. PATIENTS AND METHODS: A self-collected swab was suggested to 398 women who consulted between 15 and 33 weeks of gestation in three different centres. Gram stain evaluation using Nugent criteria was used for the diagnosis of bacterial vaginosis. RESULTS: Three hundred and forty-one women agreed to take part in the study (86%). The quality of the swabs was satisfactory in 93% of the cases. Concerning the 15 non-interpretable slides, the cellular and bacterial density was too poor, owing to a poor quality or a low vaginal flora. Thirty-one women (9%) had a bacterial vaginosis--Nugent score included between 7 and 10--and this frequency did not vary according to the centre. Thirty-five women (10%) had an intermediate flora--score between 4 and 6--and this result varied from 2 to 12% depending on the centre, but the difference was not significant. DISCUSSION AND CONCLUSION: Self-collected swabs to detect bacterial vaginosis are well accepted by most of pregnant women, and the quality of the swabs seems to be satisfactory. In case vaginal flora is intermediate--between 4 and 6--the interpretation of the slides could be difficult.

Characterization of the Acinetobacter baumannii Fur regulator: cloning and sequencing of the fur homolog gene.

Growth kinetics, siderophore activity and iron-regulated bacterial proteins of Acinetobacter baumannii BM2580 were studied in iron-restricted and iron-supplemented chemically defined media. Iron-regulated outer membrane proteins of 75 kDa and 80 kDa were expressed under iron-restricted conditions. Cloning and sequencing of the complete iron-uptake regulatory (fur) gene from A. baumannii BM2580 is reported for the first time. This gene is preceded by a single autoregulated promoter whose -10 region overlaps the Fur binding site. The open reading frame identified encodes a polypeptide consisting of 145 amino acids. The fur gene is followed by a divergent open reading frame coding for the C-terminus of a putative PilU protein. Sequence analysis indicates that the Fur protein of A. baumannii was 63% identical to the Escherichia coli Fur protein.

Effects of host iron transport compounds on growth kinetics and outer-membrane protein expression of Bilophila wadsworthia.

Since the environmental iron concentration has emerged as an important attribute in the expression of bacterial virulence, the purpose of this study was to determine the effects of transferrin, lactoferrin, heme compounds, and inorganic iron sources (ferric and ferrous sulfate) on the growth of Bilophila wadsworthia and to study its outer membrane composition when grown under these different simulated in vivo conditions. Lactoferrin, transferrin, hemin and hemoglobin supported full growth of the bacteria in media lacking other iron sources. Bilophila wadsworthia was also capable of growing in the presence of ferrous and ferric sulfate. Profiles obtained by SDS-PAGE showed two iron-regulated outer membrane proteins (IROMPs) of 190 kDa and 88 kDa. The 190 kDa was susceptible to proteinase K cleavage in whole cells, indicating its exposure at the cell surface. These two major IROMPs were expressed in iron-restricted media supplemented with iron-bound organic sources and repressed by the addition of inorganic iron sources.

Siderophore production by Staphylococcus aureus and identification of iron-regulated proteins.

Siderophore activity of Staphylococcus aureus was detected in an iron-restricted chemically defined medium. The molecular mass of this siderophore, called aureochelin, was 577 Da. Surface-associated proteins of 120, 88, 57, 35, and 33 kDa were mainly expressed under iron restriction conditions. Results showed a relationship between siderophore production and the existence of the 120- and 88-kDa proteins. Western blotting of surface-associated proteins revealed that these proteins were recognized both by patients sera and polyclonal rabbit serum.