A multi-site assessment of knowledge of Ebola virus disease among health workers in south-west Nigeria

Objective: Nigeria may have been certified free from Ebola Virus Disease (EVD) by the World Health Organization, but not without its aftermath on many, especially among health workers who came in contact with the infected during the West African outbreak in 2014.This study was conducted among health workers in three tertiary hospitals in South-West Nigeria. It aimed at assessing their knowledge of EVD in a bid to forestall future contagion from patients.Method: 600 consenting participants selected through two-stage sampling method were involved in the study. Primary data was retrieved through self-administered questionnaire.Results: Majority (84.0%) of the participants knew that EVD can be contacted through blood and bodily fluid of an infected person, (78.0%) knew that EVD can be prevented by avoiding contact with an infected person, while (76.0%) identified bleeding from orifices as one of the signs of EVD. However, (6.0%) of the participants did not know how EVD can be prevented.Conclusion: Result showed that participants have average knowledge of EVD and therefore, are not adequately informed of EVD. The study recommended wider dissemination of adequate information on EVD among health workers in tertiary hospitals to forestall future contagion of the infection from patients.Keywords: Knowledge, EVD, Contagion, Outbreak, Prevention, Bleedin

SH2-Dependent Autophosphorylation within the Tec Family Kinase Itk

The Tec family kinase, Itk (interleukin-2 tyrosine kinase), undergoes an in cis autophosphorylation on Y180 within its Src homology 3 (SH3) domain. Autophosphorylation of the Itk SH3 domain by the Itk kinase domain is strictly dependent on the presence of the intervening Src homology 2 (SH2) domain. A direct docking interaction between the Itk kinase and SH2 domains brings the Itk SH3 domain into the active site where Y180 is then phosphorylated. We now identify the residues on the surface of the Itk SH2 domain responsible for substrate docking and show that this SH2 surface mediates autophosphorylation in the full-length Itk molecule. The canonical phospholigand binding site on the SH2 domain is not involved in substrate docking, instead the docking site consists of side chains from three loop regions (AB, EF and BG) and part of the βD strand. These results are extended into Btk (Bruton\u27s tyrosine kinase), a Tec family kinase linked to the B-cell deficiency X-linked agammaglobulinemia (XLA). Our results suggest that some XLA-causing mutations might impair Btk phosphorylation