Dual tension: Lassa fever and COVID-19 in Nigeria

Lassa fever is a viral hemorrhagic, zoonotic disease that is a continuous health issue in West African countries such as Sierra Leone, Liberia, Guinea and Nigeria [1]. Ingestion and inhalation are the most common ways of transmission of Lassa fever. Patients generally get infected due to an exposure to food or household items which are contaminated with urine or droppings of infected Mastomys rodents. Lassa fever was first discovered in Lassa town, Borno State in Nigeria. It causes around 1000,000 – 300,000 infections each year with approximately 5,000 deaths in Nigeria [1]. In 2020, 70 deaths have been reported in 26 Nigerian states and the Federal Capital Territory. Among all those cases, 75% were from Edo, Ondo, and Ebonyi [2]. As of May 2020, Nigeria has recorded 991 confirmed cases and 191 deaths with case fatality ratio of 19.3% [3]. To prevent and mitigate the negative impact of Lassa Fever, the Nigeria Center for Disease Control (NCDC) has formed an interdisciplinary, multi-partner technical team to control outbreaks in affected Nigerian states

Functional activity of GSSM™ and reassembled combination antibody variants

() The top 10 antibody variants from the GSSM™ as determined by functional spike ELISA normalized to the relative expression of the antibody variant. The specific activity for each antibody was normalized to the wild-type (WT) control antibody (WT: chimeric antibody, 4049Fab14). () Purified antibody candidates from (A) tested in the plaque reduction neutralization test (PRNT). The number of plaques resulting in 50 and 80% neutralization is noted. Statistical analysis at the approximate WT antibody concentration for 80% neutralization (0.78 µg/ml) indicates better neutralization (i.e. fewer plaques) for 51E7 and 52G3 ( < 0.02 and < 0.03, respectively). () Top 10 antibody variants from the combination library (containing the best GSSM™ mutants placed in the best framework backbones) determined as described in (A). () Purified antibody candidates from (C) tested in the PRNT. Data was not collected for one of the 10 variants. Statistical analysis at the WT antibody concentration for 80% neutralization (1.56 µg/ml) indicates better neutralization (i.e. fewer plaques) for several antibodies (i.e. < 0.02 for 2978/15, 2992/15, 2978/10, 2702/10; < 0.03 for 2703/10; < 0.04 for 2703/15 and < 0.05 for 2699/10). Duplicates of each variant were assayed in the ELISA and PRNT experiments.<p><b>Copyright information:</b></p><p>Taken from "Rapid discovery and optimization of therapeutic antibodies against emerging infectious diseases"</p><p></p><p>Protein Engineering, Design and Selection 2008;21(8):495-505.</p><p>Published online 13 May 2008</p><p>PMCID:PMC2461042.</p><p>© 2008 The Author(s)</p

Functional activity of human framework reassembly (HuFR™) antibody variants

() The top 10 antibody variants from the heavy chain library as determined by functional spike ELISA normalized to the relative expression of antibody variant. The specific activity for each antibody was further normalized to the wild-type (WT) control antibody (i.e. WT: chimeric antibody, 4049Fab14). () The top 10 antibody variants from the light chain library determined as described in (A). Numbers within bars indicate the corresponding heavy chains. () Purified antibody candidates were tested in the plaque reduction neutralization test (PRNT). The number of plaques resulting in 50 and 80% neutralization is noted. Statistical analysis at the approximate WT antibody concentration for 80% neutralization (0.78 µg/ml) indicates better neutralization (i.e. fewer plaques) for 61G4 ( < 0.04). Duplicates of each variant were assayed in the ELISA and PRNT experiments.<p><b>Copyright information:</b></p><p>Taken from "Rapid discovery and optimization of therapeutic antibodies against emerging infectious diseases"</p><p></p><p>Protein Engineering, Design and Selection 2008;21(8):495-505.</p><p>Published online 13 May 2008</p><p>PMCID:PMC2461042.</p><p>© 2008 The Author(s)</p

Representative ELISA data of SARS-CoV-reactive Fabs isolated by DNA display

() Zinc finger-Fab fusion proteins analyzed in an ELISA using the spike protein as a capture reagent on 48 wells of a 96-well Maxisorp plates. Bovine serum albumin coated on the remaining 48 wells was used to determine specificity of binding. () Relative specific activity is the functional activity from Fig. A normalized to the amount of fusion protein determined using an ELISA measuring relative expression levels.<p><b>Copyright information:</b></p><p>Taken from "Rapid discovery and optimization of therapeutic antibodies against emerging infectious diseases"</p><p></p><p>Protein Engineering, Design and Selection 2008;21(8):495-505.</p><p>Published online 13 May 2008</p><p>PMCID:PMC2461042.</p><p>© 2008 The Author(s)</p

A rare variant in APOC3 is associated with plasma triglyceride and VLDL levels in Europeans

The analysis of rich catalogues of genetic variation from population-based sequencing provides an opportunity to screen for functional effects. Here we report a rare variant in APOC3 (rs138326449-A, minor allele frequency ∼0.25% (UK)) associated with plasma triglyceride (TG) levels (-1.43 s.d. (s.e.=0.27 per minor allele (P-value=8.0 × 10 -8)) discovered in 3,202 individuals with low read-depth, whole-genome sequence. We replicate this in 12,831 participants from five additional samples of Northern and Southern European origin (-1.0 s.d. (s.e.=0.173), P-value=7.32 × 10 -9). This is consistent with an effect between 0.5 and 1.5 mmol l -1 dependent on population. We show that a single predicted splice donor variant is responsible for association signals and is independent of known common variants. Analyses suggest an independent relationship between rs138326449 and high-density lipoprotein (HDL) levels. This represents one of the first examples of a rare, large effect variant identified from whole-genome sequencing at a population scale