There has considerable interest in bringing low/middle-income countries (LMIC) scientists into discussions on Open Data – both as contributors and users. The establishment of in situ data sharing practices within LMIC research institutions is vital for the development of an Open Data landscape in the Global South. Nonetheless, many LMICs have significant challenges – resource provision, research support and extra-laboratory infrastructures. These low-resourced environments shape data sharing activities, but are rarely examined within Open Data discourse. In particular, little attention is given to how these research environments shape scientists’ perceptions of data sharing (dis)incentives. This paper expands on these issues of incentivizing data sharing, using data from a quantitative survey disseminated to life scientists in 13 countries in sub-Saharan Africa. This interrogated not only perceptions of data sharing amongst LMIC scientists, but also how these are connected to the research environments and daily challenges experienced by them. The paper offers a series of analysis around commonly cited (dis)incentives such as data sharing as a means of improving research visibility; sharing and funding; and online connectivity. It identifies key areas that the Open Data community need to consider if true openness in research is to be established in the Global South.
Background: Human immunodeficiency virus type 1 (HIV-1) has infected more than 40 million people worldwide, mainly in sub-Saharan Africa. The high prevalence of HIV-1 subtype C in southern Africa necessitates the development of cheap, effective vaccines. One means of production is the use of plants, for which a number of different techniques have been successfully developed. HIV-1 Pr55Gag is a promising HIV-1 vaccine candidate: we compared the expression of this and a truncated Gag (p17/p24) and the p24 capsid subunit inNicotianaspp. using transgenic plants and transient expression viaAgrobacterium tumefaciensand recombinant tobamovirus vectors. We also investigated the influence of subcellular localisation of recombinant protein to the chloroplast and the endoplasmic reticulum (ER) on protein yield. We partially purified a selected vaccine candidate and tested its stimulation of a humoral and cellular immune response in mice.Results: Both transient and transgenic expression of the HIV antigens were successful, although expression of Pr55Gag was low in all systems; however, theAgrobacterium-mediated transient expression of p24 and p17/p24 yielded best, to more than 1 mg p24/kg fresh weight. Chloroplast targeted protein levels were highest in transient and transgenic expression of p24 and p17/p24. The transiently-expressed p17/p24 was not immunogenic in mice as a homologous vaccine, but it significantly boosted a humoral and T cell immune response primed by agagDNA vaccine, pTHGagC.Conclusion: Transient agroinfiltration was best for expression of all of the recombinant proteins tested, and p24 and p17/p24 were expressed at much higher levels than Pr55Gag. Our results highlight the usefulness of plastid signal peptides in enhancing the production of recombinant proteins meant for use as vaccines. The p17/p24 protein effectively boosted T cell and humoral responses in mice primed by the DNA vaccine pTHGagC, showing that this plant-produced protein has potential for use as a vaccine.
1 January 2017 in Environmental Technology Reviews
Developing countries are faced with a serious challenge of wastewater management that has resulted in large volumes of partially, or untreated wastewater being released into the environment. In Southern Africa, the wastewater challenge is exacerbated by the dramatic rate of urbanisation which has placed unprecedented pressure on the installed wastewater treatment services in many urban areas. Contamination of water bodies by urban wastewaters is frequently implicated in the high incidences of diarrheal diseases that have affected most developing countries. Phytoremediation, using constructed wetlands, has emerged as a promising alternative or additional treatment measure to conventional methods. Despite the promise offered by phytoremediation, the exact mechanisms of pathogen removal by the macrophytes are still being debated. Frequent and validated mechanisms include: (i) attachment, adsorption, sedimentation and mechanical filtration by plant roots, (ii) plant microbe interaction within biofilms and (iii) oxidation, UV radiation and exposure to biocides. However, research has remained silent about the possibility of pathogen removal through uptake of-, and inhibition of, pathogens in the plant body, and inhibition of the microorganisms by plant exudates. Research is therefore needed to bridge the knowledge gap and to customise phytoremediation technologies to the wastewater treatment challenges that developing countries continue to face.
Pantothenate (vitamin B5) is a water-soluble vitamin essential for the synthesis of CoA and ACP (acyl-carrier protein, cofactors in energy yielding reactions including carbohydrate metabolism and fatty acid synthesis. Pantothenate is synthesized de novo by plants and micro-organisms; however, animals obtain the vitamin through their diet. Utilizing our knowledge of the pathway in Escherichia coli, we have discovered and cloned genes encoding the first and last enzymes of the pathway from Arabidopsis, panB1, panB2 and panC. It is unlikely that there is a homologue of the E. coli panD gene, therefore plants must make β-alanine by an alternative route. Possible candidates for the remaining gene, panE, are being investigated. GFP (green fluorescent protein) fusions of the three identified plant enzymes have been generated and the subcellular localization of the enzymes studied. Work is now being performed to elucidate expression patterns of the transcripts and characterize the proteins encoded by these genes.
7 February 2014 in The Journal of Infectious Diseases
Rabies post-exposure prophylaxis (PEP) currently comprises administration of rabies vaccine together with rabies immunoglobulin (RIG) of either equine or human origin. In the developing world, RIG preparations are expensive, often in short supply, and of variable efficacy. Therefore, we are seeking to develop a monoclonal antibody cocktail to replace RIG. Here, we describe the cloning, engineering and production in plants of a candidate monoclonal antibody (E559) for inclusion in such a cocktail. The murine constant domains of E559 were replaced with human IgG1κ constant domains and the resulting chimeric mouse-human genes were cloned into plant expression vectors for stable nuclear transformation of Nicotiana tabacum. The plant-expressed, chimeric antibody was purified and biochemically characterized, was demonstrated to neutralize rabies virus in a fluorescent antibody virus neutralization assay, and conferred protection in a hamster challenge model.
The glycans on HIV-1 gp120 play an important role in shielding neutralization-sensitive epitopes from antibody recognition. They also serve as targets for lectins that bind mannose-rich glycans. In this study, we investigated the interaction of the lectin griffithsin (GRFT) with HIV-1 gp120 and its effects on exposure of the CD4-binding site (CD4bs). We found that GRFT enhanced the binding of HIV-1 to plates coated with anti-CD4bs antibodies b12 and b6 or the CD4 receptor mimetic CD4-IgG2. The average enhancement of b12 or b6 binding was higher for subtype B viruses than for subtype C, while for CD4-IgG2, it was similar for both subtypes, although lower than observed with antibodies. This GRFT-mediated enhancement of HIV-1 binding to b12 was reflected in synergistic neutralization for 2 of the 4 viruses tested. The glycan at position 386, which shields the CD4bs, was involved in both GRFT-mediated enhancement of binding and neutralization synergism between GRFT and b12. Although GRFT enhanced CD4bs exposure, it simultaneously inhibited ligand binding to the coreceptor binding site, suggesting that GRFT-dependent enhancement and neutralization utilize independent mechanisms. This study shows for the first time that GRFT interaction with gp120 exposes the CD4bs through binding the glycan at position 386, which may have implications for how to access this conserved site.