Embedding a Dedicated Sexual Health Clinic in a University's Health Services Expands Sexually Transmitted Infection Screening Options.

BACKGROUND: The primary objectives of this study were to assess utilization of sexual health services at a university's student health and wellness center and to determine whether the presence of a dedicated sexual health clinic (SHC) was associated with different utilization patterns for sexual health services when compared with primary care clinics. METHODS: This was a retrospective chart review of patients presenting to the University of Alabama at Birmingham's Student Health and Wellness Center for sexual health services between January 2015 and June 2019. Utilization of sexual health services, specifically sexually transmitted infection (STI) testing, was compared between the dedicated SHC and primary care clinics. RESULTS: A total of 3081 cases were included. There were statistically significant differences in the proportion of male individuals and populations more burdened by STI tested for STI in the SHC (i.e., persons who identify as Black and younger female individual). We also observed a higher percentage of positive gonorrhea and chlamydia test results and a greater likelihood of extragenital screening in men who have sex with men in the SHC. CONCLUSIONS: The dedicated SHC within the University of Alabama at Birmingham's Student Health and Wellness Center was associated with an increase in STI screenings. There was a significant difference between the demographics of those presenting to the SHC versus primary care clinics, proportionally more diagnoses of gonorrhea and chlamydia, and, for men who have sex with men, more extragenital screenings performed in the SHC. These findings suggest that there may be a benefit of an embedded SHC in college and university health and wellness centers.

Structures of Abeta-related peptide--monoclonal antibody complexes.

Passive immunotherapy (PI) is being explored as a potential therapeutic against Alzheimer's disease. The most promising antibodies (Abs) used in PI target the EFRH motif of the Abeta N-terminus. The monoclonal anti-Abeta Ab PFA1 recognizes the EFRH epitope of Abeta. PFA1 has a high affinity for Abeta fibrils and protofibrils (0.1 nM), as well as good affinity for Abeta monomers (20 nM). However, PFA1 binds the toxic N-terminally modified pyroglutamate peptide pyro-Glu3-Abeta with a 77-fold loss in affinity compared to the WT Abeta(1-8). Furthermore, our earlier work illustrated PFA1's potential for cross-reactivity. The receptor tyrosine kinase Ror2, which plays a role in skeletal and bone formation, possesses the EFRH sequence. PFA1 Fab binds the Ror2(518-525) peptide sequence REEFRHEA with a 3-fold enhancement over WT Abeta(1-8). In this work, the crystal structures of the hybridoma-derived PFA1 Fab in complex with pyro-Glu3-Abeta peptide and with a cross-reacting peptide from Ror2 have been determined at resolutions of 1.95 and 2.7 A, respectively. As with wild-type Abeta, these peptides bind to the Fab via a combination of charge- and shape-complementarity, hydrogen-bonding, and hydrophobic interactions. Comparison of the structures of the four peptides Abeta(1-8), Grip1, pyro-Glu3-Abeta(3-8), and Ror2 in complex with PFA1 shows that the greatest conformational flexibility occurs at residues 2 to 3 and 8 of the peptide. These structures provide a molecular basis of the specificity tolerance of PFA1 and its ability to recognize Abeta N-terminal heterogeneity. The structures provide clues to improving mAb specificity and affinity for pyroglutamate Abeta.