Social and healthcare students' competence in patient-oriented care enhanced during interprofessional practice: A scoping review.

AIM: This scoping review aimed to synthesise the findings of previous literature related to social and healthcare students' competence in patient-oriented care in interprofessional practice by attending multidisciplinary student teams. BACKGROUND: Learning about patient-oriented care requires the comprehensive consideration of patients' physical, emotional, social and economic aspects to offer the best need-based care. Multidisciplinary student teams in the clinical practice may support learning patient-oriented care; however, the current knowledge is fragmented. DESIGN: Scoping review METHODS: Data (N = 1548) were gathered from four databases, PubMed, MEDLINE, SocIndex and CINAHL, without start-date limitation until the end of December 2022. One article was found on the publisher's webpage recommendations. The selected studies (N = 15) answered the research questions and met the inclusion criteria. Quality assessment of the studies was conducted using the Joanna Briggs Institute (JBI) Quality Assessment Checklist. A thematic analysis process was used for data extraction and synthesis of results. RESULTS: Perspectives on patient-oriented care competencies were analysed for both students and patients cared for by a multidisciplinary student team. The themes described students' profound understanding of professional roles and responsibilities in patient-oriented care, collaborative patient-oriented care skills, improved interprofessional communication and reported patient experiences. CONCLUSIONS: Interprofessional practice versatility develops students' competence in patient-oriented care. Guaranteeing patient-oriented care requires a broad understanding of patients' comprehensive care needs, which can be addressed through multidisciplinary collaboration. Patients' experiences toward interprofessional student practice are mainly positive. Further research is needed to assess the impact of different interprofessional education methods on students' patient-oriented care competence using valid instruments and the long-term effects of students' competence in patient-oriented care.

The Escherichia coli G-fimbrial lectin protein participates both in fimbrial biogenesis and in recognition of the receptor N-acetyl-D-glucosamine.

The gafD gene encoding the N-acetyl-D-glucosamine-specific fimbrial lectin (adhesin) protein GafD of uropathogenic Escherichia coli was cloned and subjected to genetic analysis. The corresponding gene product was isolated as a MalE fusion protein. The lectin gene was identified with the aid of deletion mutagenesis; mutations in gafD impaired either receptor binding or both receptor binding and fimbria production, depending on the mutation created. All mutants converted to wild-type expressors when complemented in trans with the cloned intact gafD gene. The predicted 354-amino-acid sequence of GafD, deduced from the nucleotide sequence, is closely related to those of the fimbria-associated F17-G and F17b-G proteins coded for by enterotoxigenic and invasive E. coli strains. Isolated GafD was shown to recognize N-acetyl-D-glucosamine by virtue of specific binding to an immobilized receptor, thus proving directly that GafD is a sugar-binding protein. Our results indicate that GafD as such is sufficient for receptor recognition and that the protein also participates in fimbrial biogenesis.

N-acetyllactosaminooligosaccharides that contain the beta-D-GlcpNAc-(1----6)-D-Gal or beta-D-GlcpNAc-(1----6)-D-GalNAc sequences reveal reduction-sensitive affinities for wheat germ agglutinin.

Affinity chromatography of unreduced oligosaccharides on a small column of immobilized wheat germ agglutinin (WGA) revealed high-binding affinities for several radiolabeled molecules containing at the reducing end either beta-D-GlcpNAc-(1----6)-D-Gal, beta-D-GlcpNAc-(1----6)-beta- D-Galp-(1----4)-D-GlcNAc, beta-D-GlcpNAc-(1----6)-beta-D-Galp-(1----4)DGlc, D-GlcpNAc-(1----3)-[beta-D-GlcpNAc-(1----6)]-D-Gal, beta-D-GlcpNAc-(1----6)- D-GalNAc, or beta-D-Galp-(1----3)-[beta-D-GlcpNAc-(1----6)]-D-GalNAc sequences. Reduction changed the binding affinities remarkably: The sequences carrying a D-galactose or 2-acetamido-2-deoxy-D-galactose residue at the reducing end lost most of their affinities, but the sequences containing a D-glucose or 2-acetamido-2-deoxy-D-glucose residue at the reducing end gained additional affinity upon reduction. These findings emphasize the role of the unreduced, 6-o-substituted D-galactose and 2-acetamido-2-deoxy-D-galactose residues for the binding of saccharides to WGA, which has been recognized previously as a lectin specific for oligosaccharides containing a 2-acetamido-2-deoxy-D-glucose or sialic acid unit. The results suggested also that WGA-agarose chromatography of alditols may become a valuable method for the fractionation of oligo-N-acetyllactosaminoglycans and related saccharides.

Wheat germ agglutinin chromatography of GlcNac beta 1-3(GlcNAc beta 1-6)Gal and GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4GlcNAc, obtained by in vitro synthesis and by partial cleavage of teratocarcinoma poly-N-acetyllactosaminoglycans.

GlcNAc beta 1-3(GlcNAc beta 1-6) [14C(U)]Gal and GlcNAc beta 1-3(GlcNAc beta 1-6)[14C(U)]Gal beta 1-4GlcNAc were prepared by in vitro synthesis. They were characterized by enzymatic sequencing, by partial acid hydrolysis, and by periodate oxidation experiments. The two saccharides were isolated also from partial acid hydrolysates of metabolically labeled poly-N-acetyllactosaminoglycans of murine embryonal carcinoma cells (line PC 13). The tetrasaccharide was retarded in a column of agarose-linked wheat germ agglutinin; the trisaccharide was strongly bound. Chromatography in this column separated the trisaccharide into two distinct peaks, which represented interconvertible molecules. Together with our previous data on linear teratocarcinoma saccharides, these findings show that affinity chromatography with immobilized wheat germ agglutinin can be advantageously used in fractionating radiolabeled oligo-N-acetyllactosaminoglycans and saccharides related to them.

The linear tetrasaccharide, Gal beta 1-4GlcNAc beta 1-6Gal beta 1-4GlcNAc, isolated from radiolabeled teratocarcinoma poly-N-acetyllactosaminoglycan resists the action of E. freundii endo-beta-galactosidase.

A novel linear tetrasaccharide, Gal beta 1-4GlcNAc beta 1-6Gal beta 1-4GlcNAc, was isolated from partial acid hydrolysates of metabolically labeled poly-N-acetyllactosaminoglycans of murine teratocarcinoma cells. It was characterized by exo-glycosidase sequencing and by mild acid hydrolysis followed by identification of all partial cleavage products. The tetrasaccharide, and likewise labelled GlcNAc beta 1-6Gal beta 1-4GlcNAc, resisted the action of endo-beta-galactosidase (EC 3.2.1.103) from E. freundii at a concentration of 125 mU/ml, while the isomeric, radioactive teratocarcinoma saccharides Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4GlcNAc and GlcNAc beta 1-3Gal beta 1-4GlcNAc were cleaved in the expected manner.