COVID-19 and practice transformation: Building an office-based opioid treatment program in a family medicine residency practice.

INTRODUCTION: This brief report describes how a family medicine residency practice (FMRP) leveraged a resident-led quality improvement project and a grant-funded Addiction Integrated Care Team (AICT) to initiate an office-based opioid treatment (OBOT) program to provide medications for opioid use disorder during the COVID-19 pandemic. METHOD: In 2020, the practice experienced four disruptors that shifted motivation for practice development: (a) The COVID-19 pandemic demanded rapid change in primary care processes/staffing, including pivoting to telehealth/remote practice. (b) The practice's transition to a federally qualified community health center model meant a shift in organizational priorities that required offering OBOT services. (c) External grant resources became available through the AICT program to support practice core for OBOT, and 10 implementation strategies were utilized. (d) A resident champion implemented an OBOT quality improvement project. RESULTS: These efforts resulted in the practice offering the OBOT program and 18 patients receiving OBOT from January 2020 to February 2021, with 10 of 18 patients engaged for 12 months or longer. Further, the cumulative adoption and reach from January 2020 through September 2022 was 15 faculty and 14 residents becoming prescribers and 101 patients served within the OBOT program, respectively. DISCUSSION: FMRPs striving for significant practice transformation, such as implementing an OBOT program during a pandemic, may benefit from synergistic guidance and resources including established theory, strategies from the implementation science literature, and resident-led quality improvement efforts. (PsycInfo Database Record (c) 2023 APA, all rights reserved).

Self-association motifs in the enteroaggregative Escherichia coli heat-resistant agglutinin 1.

The heat-resistant agglutinin 1 (Hra1) is an integral outer membrane protein found in strains of Escherichia coli that are exceptional colonizers. Hra1 from enteroaggregative E. coli strain 042 is sufficient to confer adherence to human epithelial cells and to cause bacterial autoaggregation. Hra1 is closely related to the Tia invasin, which also confers adherence, but not autoaggregation. Here, we have demonstrated that Hra1 mediates autoaggregation by self-association and we hypothesize that at least some surface-exposed amino acid sequences that are present in Hra1, but absent in Tia, represent autoaggregation motifs. We inserted FLAG tags along the length of Hra1 and used immune-dot blots to verify that four in silico-predicted outer loops were indeed surface exposed. In Hra1 we swapped nine candidate motifs in three of these loops, ranging from one to ten amino acids in length, to the corresponding sequences in Tia. Three of the motifs were required for Hra1-mediated autoaggregation. The database was searched for other surface proteins containing these motifs; the GGXWRDDXK motif was also present in a surface-exposed region of Rck, a Salmonella enterica serotype Typhimurium complement resistance protein. Cloning and site-specific mutagenesis demonstrated that Rck can confer weak, GGXWRDDXK-dependent autoaggregation by self-association. Hra1 and Rck appear to form heterologous associations and GGXWRDDXK is required on both molecules for Hra1-Rck association. However, a GGYWRDDLKE peptide was not sufficient to interfere with Hra1-mediated autoaggregation. In the present study, three autoaggregation motifs in an integral outer membrane protein have been identified and it was demonstrated that at least one of them works in the context of a different cell surface.

The heat-resistant agglutinin family includes a novel adhesin from enteroaggregative Escherichia coli strain 60A.

Heat-resistant agglutinin 1 (Hra1) is an accessory colonization factor of enteroaggregative Escherichia coli (EAEC) strain 042. Tia, a close homolog of Hra1, is an invasin and adhesin that has been described in enterotoxigenic E. coli. We devised a PCR-restriction fragment length polymorphism screen for the associated genes and found that they occur among 55 (36.7%) of the enteroaggregative E. coli isolates screened, as well as lower proportions of enterotoxigenic, enteropathogenic, enterohemorrhagic, and commensal E. coli isolates. Overall, 25%, 8%, and 3% of 150 EAEC strains harbored hra1 alone, tia alone, or both genes, respectively. One EAEC isolate, 60A, produced an amplicon with a unique restriction profile, distinct from those of hra1 and tia. We cloned and sequenced the full-length agglutinin gene from strain 60A and have designated it hra2. The hra2 gene was not detected in any of 257 diarrheagenic E. coli isolates in our collection but is present in the genome of Salmonella enterica serovar Heidelberg strain SL476. The cloned hra2 gene from strain 60A, which encodes a predicted amino acid sequence that is 64% identical to that of Hra1 and 68% identical to that of Tia, was sufficient to confer adherence on E. coli K-12. We constructed an hra2 deletion mutant of EAEC strain 60A. The mutant was deficient in adherence but not autoaggregation or invasion, pointing to a functional distinction from the autoagglutinin Hra1 and the Tia invasin. Hra1, Tia, and the novel accessory adhesin Hra2 are members of a family of integral outer membrane proteins that confer different colonization-associated phenotypes.