Retrospective Study on the Effect of the Timing of Exposure on Confidence Level in Applying to Physical Medicine and Rehabilitation Residency Programs.

ABSTRACT: Residency specialty choice, a complex decision-making process, is often influenced by confidence level built upon knowledge, experience, and fit with the specialty. Despite the need for physiatrists with population growth, especially people with disability and older patients, limited growth in the number of residency positions and delayed exposure to the field of physical medicine and rehabilitation potentially contribute to a lack of confidence in pursuing physical medicine and rehabilitation. Early introduction to a specialty has been shown to impact specialty selection. Thus, this study aims to explore the impact of timing of exposure to physiatry on the confidence level of physical medicine and rehabilitation residents in their specialty choice. A survey for current physical medicine and rehabilitation residents was developed and distributed to residency program directors with a request to forward it to all residents. The response rate was low at 13%; however, the results provide a window into the experience of today's medical and premedical students. Interestingly, of the 175 respondents, a similar number reported first exposure to physiatry during third year and before medical school. In addition, earlier exposure was associated with higher confidence levels in specialty choice, the most powerful factor being the exposure to the specialty before starting medical school or during the preclinical years in medical school. These findings highlight opportunities to improve the physiatry workforce by providing earlier exposure to the specialty, even before medical school. Based on the results of the survey and ongoing discussions among medical students, residents, and faculty leaders, the authors review current recruitment efforts and new ideas.

Reduction of Injection-Related Risk Behaviors After Emergency Implementation of a Syringe Services Program During an HIV Outbreak.

OBJECTIVE: To describe injection-related HIV risk behaviors preimplementation and postimplementation of an emergency syringe services program (SSP) in Scott County, Indiana, after an HIV outbreak among persons who inject drugs (PWID). DESIGN: Mixed methods retrospective pre-post intervention analysis. METHODS: We analyzed routine SSP program data collected at first and most recent visit among clients with ≥2 visits, ≥7 days apart from April 4 to August 30, 2015, to quantify changes in injection-related risk behaviors. We also analyzed qualitative data collected from 56 PWID recruited in Scott County to understand factors contributing to these behaviors. RESULTS: SSP clients included in our analysis (n = 148, 62% of all SSP clients) reported significant (P < 0.001) reductions over a median 10 weeks (range 1-23) in syringe sharing to inject (18%-2%) and divide drugs (19%-4%), sharing other injection equipment (eg, cookers) (24%-5%), and number of uses of the same syringe [2 (interquartile range: 1-4) to 1 (interquartile range: 1-1)]. Qualitative study participants described access to sterile syringes and safer injection education through the SSP, as explanatory factors for these reductions. Injection frequency findings were mixed, but overall suggested no change. The number of syringes returned by SSP clients increased from 0 at first visit to median 57. All qualitative study participants reported using sharps containers provided by the SSP. CONCLUSIONS: Analyses of an SSP program and in-depth qualitative interview data showed rapid reduction of injection-related HIV risk behaviors among PWID post-SSP implementation. Sterile syringe access as part of comprehensive HIV prevention is an important tool to control and prevent HIV outbreaks.

Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes.

Glyceraldehyde 3-phosphate dehydrogenase or GAPDH is an evolutionarily conserved glycolytic enzyme. It catalyzes the two step oxidative phosphorylation of D-glyceraldehyde 3-phosphate into 1,3-bisphosphoglycerate using inorganic phosphate and NAD+ as cofactor. GAPDH of Group B Streptococcus is a major virulence factor and a potential vaccine candidate. Moreover, since GAPDH activity is essential for bacterial growth it may serve as a possible drug target. Crystal structures of Group B Streptococcus GAPDH in the apo-form, two different binary complexes and the ternary complex are described here. The two binary complexes contained NAD+ bound to 2 (mixed-holo) or 4 (holo) subunits of the tetrameric protein. The structure of the mixed-holo complex reveals the effects of NAD+ binding on the conformation of the protein. In the ternary complex, the phosphate group of the substrate was bound to the new Pi site in all four subunits. Comparison with the structure of human GAPDH showed several differences near the adenosyl binding pocket in Group B Streptococcus GAPDH. The structures also reveal at least three surface-exposed areas that differ in amino acid sequence compared to the corresponding areas of human GAPDH.

Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a conserved cytosolic enzyme, which plays a key role in glycolysis. GAPDH catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate using NAD or NADP as a cofactor. In addition, GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate. Here, the crystal structure of GBS GAPDH from Streptococcus agalactiae in complex with NAD is reported at 2.46 Šresolution. Although the overall structure of GBS GAPDH is very similar to those of other GAPDHs, the crystal structure reveals a significant difference in the area spanning residues 294-307, which appears to be more acidic. The amino-acid sequence of this region of GBS GAPDH is also distinct compared with other GAPDHs. This region therefore may be of interest as an immunogen for vaccine development.