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1.
Br J Nurs ; 30(7): 428-432, 2021 Apr 08.
Artículo en Inglés | MEDLINE | ID: mdl-33830792

RESUMEN

This article describes nurse education with the Open University in Scotland (OUiS). Although there are problems with nurse recruitment and retention across the UK, in Scotland the landscape is somewhat different, with greater support for students required in remote and rural areas. Despite these challenges, the OUiS continues to recruit to the commissioned numbers of places. OUiS nursing students are primarily health care support workers who are a key group within the health and social care workforce but historically have faced many challenges in developing clear career pathways into nursing. At the heart of the OU is the fundamental recognition of distance online pedagogy, complemented by work-based learning support by employers. Partnership working between the OU, employers and education commissioners is crucial to its success.


Asunto(s)
Educación en Enfermería , Universidades , Educación en Enfermería/tendencias , Predicción , Humanos , Escocia
2.
Mol Microbiol ; 43(4): 931-43, 2002 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-11929543

RESUMEN

We have identified a gene, lpt-3, that is required for the addition of phosphoethanolamine to the 3-position (PEtn-3) on the beta-chain heptose (HepII) of the inner core lipopolysaccharide (LPS) of Neisseria meningitidis (Nm). The presence of this PEtn-3 substituent is characteristic of the LPS of a majority ( approximately 70%) of hypervirulent Nm strains, irrespective of capsular serogroup, and is required for the binding of a previously described monoclonal antibody (mAb B5) to a surface-accessible epitope. All strains of Nm that have PEtn-3 possess the lpt-3 gene. In some lpt-3-containing strains, the 3-position on HepII is preferentially substituted by glucose instead of PEtn, the result of lgtG phase variation mediated by slippage of a homopolymeric tract of cytidines. Inactivation of lpt-3 resulted in loss of PEtn-3, lack of reactivity with mAb B5 and conferred relative resistance to bactericidal killing and opsonophagocytosis by mAb B5 in vitro. Thus, the identification of lpt-3 has facilitated rigorous genetic, structural and immunobiological definition of an immunodominant epitope that is a candidate immunogen for inclusion in an LPS-based vaccine to protect against invasive meningococcal disease.


Asunto(s)
Proteínas Bacterianas/metabolismo , Etanolaminas/metabolismo , Genes Bacterianos/fisiología , Lipopolisacáridos/metabolismo , Neisseria meningitidis/metabolismo , Fosfotransferasas (Aceptor de Grupo Alcohol)/metabolismo , Anticuerpos Monoclonales/metabolismo , Proteínas Bacterianas/genética , Mutagénesis Insercional , Neisseria meningitidis/genética , Fagocitosis , Fenotipo , Fosfotransferasas (Aceptor de Grupo Alcohol)/genética
3.
Gene ; 284(1-2): 133-40, 2002 Feb 06.
Artículo en Inglés | MEDLINE | ID: mdl-11891054

RESUMEN

Lipopolysaccharide (LPS) is important for the virulence of Neisseria meningitidis, and is the target of immune responses. We took advantage of a monoclonal antibody (Mab B5) that recognises phosphoethanolamine (PEtn) attached to the inner core of meningococcal LPS to identify genes required for the addition of PEtn to LPS. Insertional mutants that lost Mab B5 reactivity were isolated and characterised, but failed to yield genes directly responsible for PEtn substitution. Subsequent genetic linkage analysis was used to define a region of DNA containing a single intact open reading frame which is sufficient to confer B5 reactivity to a B5 negative meningococcal isolate. The results provide an initial characterisation of the genetic basis of a key, immunodominant epitope of meningococcal LPS.


Asunto(s)
Etanolaminas/metabolismo , Genes Bacterianos/genética , Lipopolisacáridos/metabolismo , Neisseria meningitidis/genética , Anticuerpos Monoclonales/inmunología , ADN Bacteriano/genética , ADN Bacteriano/inmunología , Etanolaminas/inmunología , Ligamiento Genético , Lipopolisacáridos/inmunología , Mutación , Neisseria meningitidis/inmunología , Neisseria meningitidis/metabolismo
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