ABSTRACT
The SulA protein of Escherichia coli and related bacteria interacts directly with FtsZ, blocking cell division by disrupting Z-ring formation, yet the precise mechanism remains not fully understood. Previous demonstrations of Pseudomonas aeruginosa SulA's dimerization capability were confined to X-ray crystallography and lacked confirmation under in vivo conditions. Additionally, uncertainty persisted regarding the dimerization potential of E. coli's SulA protein. This paper employs a bacterial two-hybrid system to establish that both P. aeruginosa and E. coli SulA proteins indeed possess the capacity for dimerization.
Subject(s)
Escherichia coli Proteins , Escherichia coli , Escherichia coli/metabolism , Pseudomonas aeruginosa , Bacterial Proteins/chemistry , Dimerization , Escherichia coli Proteins/metabolism , Cell DivisionABSTRACT
Based on the success of the Sabin2-based vaccine, a next-generation nOPV2 poliovirus vaccine has been developed. For epidemic monitoring and conducting epidemiological investigations, it is necessary to have a diagnostic assay with the ability to differentiate this variant from others. Here we describe such a real-time RT-PCR assay. The region with the cre insertion in the 5'-UTR was chosen as the target, and the limit of detection was 103 copies/mL (2.5×103 copies/mL using Probit analysis) determined using armored RNA particles. Sensitivity and specificity were 86.28 - 100â¯% and 76.84 - 100â¯%, respectively (with 95â¯% CI). Thus, this method can be effectively used when it is necessary to make a differential diagnosis of poliovirus strains.