ABSTRACT
Silver diamine fluoride (SDF) is a clear, odourless liquid indicated for desensitisation of non-carious tooth lesions and molar incisor hypomineralisation. It is also useful for arresting carious lesions in adults and children who are high caries-risk and/or have difficult-to-control, progressing carious lesions, those who are unable to tolerate invasive treatment, elderly populations, and those who are medically compromised or have additional care and support needs. SDF may be used to manage lesions that are too extensive to restore but not associated with pain and/or infection. This can be important particularly where extractions might be contra-indicated for medical or behavioural reasons. This paper summarises the global evidence for the effectiveness and safety of SDF, describes what it is, its mechanisms of action and presents recommendations on how to use it. There are details on indications/contra-indications and risks/benefits to be considered in the use of SDF also discussion of how to approach SDF's side effect of black staining of carious tooth tissue. We give an example of an information sheet (Appendix S1, see online supplementary information) that may be used when discussing SDF with patients, particularly for primary teeth in children, but adaptable for the permanent dentition and for adults.
Subject(s)
Cariostatic Agents , Dental Caries , Adult , Aged , Child , Fluorides, Topical , Humans , Quaternary Ammonium Compounds , Silver CompoundsABSTRACT
We analyzed the nuclear trafficking ability of Gag proteins from six retroviral genera. Contrary to a previous report, human immunodeficiency virus type 1 (HIV-1) Gag showed no propensity to cycle through the nucleus. The only Gag protein that displayed CRM1-dependent nuclear cycling was that of Rous sarcoma virus (RSV). Surprisingly, this cycling could be eliminated without compromising infectivity by replacing the RSV Gag N-terminal matrix (MA) domain with HIV MA.
Subject(s)
Gene Products, gag/metabolism , Karyopherins/metabolism , Receptors, Cytoplasmic and Nuclear/metabolism , Retroviridae/metabolism , Animals , Cell Line , Cell Nucleus/metabolism , Gene Order , Gene Products, gag/genetics , Humans , Protein Transport , Proviruses/metabolism , Retroviridae/genetics , Exportin 1 ProteinABSTRACT
The cytoplasmic tail domain (CTD) of retroviral envelope (Env) proteins has been implicated in modulating Env incorporation into viral particles. We generated a panel of murine leukemia virus (MLV) Env mutants and analyzed their ability to be recruited to human immunodeficiency virus-1 (HIV-1) assembly sites. Surprisingly, the entire CTD was dispensable for recruitment to assembly sites, but a mutation that disrupted the furin cleavage site in Env abolished recruitment. To determine if MLV Env can show selectivity for homologous assembly sites, cells were co-transfected with both HIV-1 and MLV assembly components along with each MLV Env construct and assayed for infectious particle production. MLV Env selectively formed infectious particles with the MLV components at the expense of infectious HIV-1 infectious particle production, but truncation of the CTD progressively reduced this selectivity. Collectively these data suggest that there are two separable mechanisms that govern MLV Env recruitment to viral assembly sites.
