Background There is an imperative need for innovative interventions to identify people living with HIV and initiate them on antiretroviral therapy (ART). The objective of this study was to determine the feasibility of providing index partner/child testing of people living with HIV. Methods We trained 86 nurses and counsellors in 56 public health facilities in six high HIV burden Districts in 2017 to provide index partner/child testing (tracing and testing of partners/children of people living with HIV). We collected programmatic data including index partner/child HIV positivity by age, gender and location of testing. In sub-analyses, we evaluated factors associated with identifying HIV-positive partners and children in separate models using multivariable logistic regression. Results We tested 16,033 partners and children of index patients between October 2017 and June 2018. Most of those tested were female (61%) and 20–39 years old (39%). Overall, 6.4% were 10–14 years old, 9.5% were 15–19 years; 8% were >50 years. HIV positivity was 38% (95% CI=36%−40%). In children ages 10–14, 13% were HIV-infected (95% CI=11%−14%). In subanalyses, HIV positivity in partners was associated with their increased age (adjusted odds ratio [aOR] for increase in 5-year age category=1.21; 95% CI=1.04, 1.42), female gender (aOR=1.38; 95% CI=1.04, 1.82) and bringing the partner in for HIV testing vs. referring the partner through the provider or recommending testing to the partner (aOR=1.94, 95% CI=1.43, 2.63), adjusting for location of testing. Almost all patients diagnosed (97%) were referred to ART. Conclusion Providing index partner/child testing was feasible and we identified a very high yield when testing partners/children of index patients. Index partner/child testing should be offered to all patients living with HIV to improve case finding.

Enzymes play a powerful role as catalysts with high specificity and activity under mild environmental conditions. Significant hurdles, such as reduced solubility, reduced shelf-life, aggregate formation, and toxicity, are still ongoing struggles that scientists come across when purifying recombinant proteins. Over the past three decades, PEGylation techniques have been utilized to significantly overcome low solubility; increased protein stability, shelf-life, and bioactivity; and prevented protein aggregate formation. This review seeks to highlight the impact of PEG-based formulations that are significantly utilized to obtain favourable protein physiochemical properties. The authors further discuss other techniques that can be employed such as coexpression studies and nanotechnology-based skills to obtaining favourable protein physiochemical properties.

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Background: Reagent proteins such as DNA ligases play a central role in the global reagents market. DNA ligases are routinely used and are vital in academic and science research environments. Their major functions include sealing nicks by linking the 5’-phosphorylated end to a 3’-hydroxyl end on the phosphodiester backbone of DNA, utilizing ATP or NADP molecules as an energy source. Objective: The current study sought to investigate the role of PEGylation on the biological activity of purified recombinant DNA ligases Method: We produced two recombinant DNA ligases (Ligsv081 and LigpET30) using E. coli expression system and subsequently purified using affinity chromatography. The produced proteins were conjugated to site specific PEGylation or non-specific PEGylation. FTIR and UV-VIS spectroscopy were used to analyze secondary structures of the PEG conjugated DNA ligases. Differential scanning fluorimetry was employed to assess the protein stability when subjected various PEGylation conditions. Results: In this study, both recombinant DNA ligases were successfully expressed and purified as homogenous proteins. Protein PEGylation enhanced ligation activity, increased transformation efficiency by 2-fold for plasmid ligations and reduced the formation of protein aggregates. Conclusion: Taken together, site-specific PEGylation can potentially be explored to enhance the biological activity and stability of reagent proteins such as ligases.

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