PubMedCrossRef 46. Augustyns K, Van Aerschot A, Van Schepdael A, Urbanke C, Herdewijn P: Influence of the incorporation of (S)-9-(3,4-dihydroxybutyl)adenine on the enzymatic stability and base-pairing properties of oligodeoxynucleotides.

Nucleic Acids Res 1991, 19:2587–2593.PubMedCentralPubMedCrossRef Competing interests The authors declare that they have no conflict of interests. Authors’ contributions MO conceived the study and carried out the molecular genetic studies. MN participated in the design of the study, carried out the molecular GSI-IX genetic studies and drafted the manuscript. JK participated in the design of study and drafted the manuscript. All the authors have read and approved the final manuscript.”
“Background Autotransporter proteins are the largest known family of virulence factors expressed by Gram-negative bacteria and play prominent roles in processes such as invasion [1], serum resistance [2, 3], phospholipolysis [4–6], cytotoxicity [7], adherence [8, 9], survival within eukaryotic cells [10], intracellular motility [11], cell-to-cell aggregation [12, 13], and biofilm formation [14, 15]. These molecules display conserved structural features including an N-terminal surface-exposed domain responsible SN-38 for the biological function and a hydrophobic C-terminus that tethers the autotransporter to the outer membrane (OM). Based on the learn more structure of the C-terminus, autotransporters

can be classified as conventional or oligomeric [16–21]. The C-terminus of conventional autotransporters consists of ~300 amino acids (aa) forming 10–12 antiparallel β-strands, while that of oligomeric autotransporters is substantially shorter (~70 aa) and specifies only 4 β-strands. Because

of their structure and 3-mercaptopyruvate sulfurtransferase role in virulence, autotransporters are attractive targets for developing countermeasures against pathogenic organisms. Large portions of autotransporters are located on the bacterial surface and therefore readily accessible for recognition by the immune system. Additionally, autotransporters play important roles in pathogenesis, thus targeting them may hinder the ability to cause disease. This hypothesis is supported by several studies demonstrating the effectiveness of autotransporter-based countermeasures. For example, immunization with Neisseria meningitidis NadA elicits antibodies (Abs) binding to the bacterial surface and promoting complement-mediated killing [22, 23], which is key to protection against this organism. Antibodies against Haemophilus influenzae Hap block adherence to epithelial cells and immunization with Hap protects mice in nasopharyngeal colonization studies [24, 25]. Vaccination with the Proteus mirabilis autotransporter cytotoxin Pta yields Abs that not only reduce bacterial burden in a murine urinary tract infection model, but also neutralize the cytotoxic activity of Pta for bladder cells [26].