Isolation and characterization of malaria PfHRP2 specific V-NAR antibody fragments from immunized shark phage display library

Background Malaria rapid diagnostic tests (RDTs) represent an important antibody based immunoassay platform. Unfortunately, conventional monoclonal antibodies are subject to degradation shortening shelf lives of RDTs. The variable region of the receptor (VNAR) from shark has a potential as alternative to monoclonal antibodies in RDTs due to high thermal stability. Methods In this study, new binders derived from shark VNAR domains library were investigated. Following immunization of a wobbegong shark (Orectolobus ornatus) with three recombinant malaria biomarker proteins (PfHRP2, PfpLDH and Pvaldolase), a single domain antibody (sdAb) library was constructed from splenocytes. Target-specific VNAR phage were isolated by panning. One specific clone was selected for expression in Escherichia coli expression system, and study of binding reactivity undertaken. Results The primary VNAR domain library possessed a titre of 1.16 × 106&nbsp;pfu/mL. DNA sequence analysis showed 82.5% of isolated fragments appearing to contain an in-frame sequence. After multiple rounds of biopanning, a highly dominant clone specific to PfHRP2 was identified and selected for protein production in an E. coli expression system. Biological characterization showed the recombinant protein expressed in periplasmic has better detection sensitivity than that of cytoplasmic proteins. Assays of binding activity indicated that its reactivity was inferior to the positive control mAb C1–13. Conclusions Target-specific bacteriophage VNARs were successfully isolated after a series of immunization, demonstrating that phage display technology is a useful tool for selection of antigen binders. Generation of new binding reagents such as VNAR antibodies that specifically recognize the malaria biomarkers represents an appealing approach to improve the performance of RDTs.</p

Analysis of opportunistic two-path successive relaying in consideration of inter-relay interference

Two-path successive relaying (TPSR) improves spectral efficiency of relay under half-duplex constraint. However, when the relay pair is operating in non-orthogonal channels, the capacity of TPSR can be severely degraded by inter-relay interference (IRI). Relay selection has been proposed in the existing literature to mitigate the IRI. However, existing opportunistic TPSR (OSR) schemes limit the pool of potential relay pair choices. Eventually, the performance of existing OSR schemes is underestimated. This study proposes four OSR schemes to improve the achievable performance of OSR schemes in terms of ergodic capacity and outage probability. The proposed schemes select a pair of relays jointly from the N potential relays. This increases the pool of potential relay pairs quadratically. Acknowledging the fact that OSR is only good for certain operating conditions, adaptive schemes that dynamically switches between OSR and opportunistic half-duplex relaying (OHR) are proposed. The simulation results show that the proposed schemes outperform the existing OSR, OHR and full-duplex relaying schemes significantly. The asymptotic ergodic capacity analysis of the proposed schemes increases logarithmically with the quadratic of N. The diversity and multiplexing tradeoff analysis reveals that the proposed schemes achieve the full diversity and multiplexing gain given a large number of potential relays

Generating hardware from OpenMP programs

10.1109/FPT.2006.270297Proceedings - 2006 IEEE International Conference on Field Programmable Technology, FPT 200673-8

Improved white-light reconstruction of shearograms for simultaneous measurement of displacement derivatives

10.1088/0957-0233/5/10/016Measurement Science and Technology5101303-130

Functionalized curcumin analogs as potent modulators of the Wnt/β-catenin signaling pathway

10.1016/j.ejmech.2013.10.073European Journal of Medicinal Chemistry7167-80EJMC

Validation of prediction equations for resting energy expenditure in Singaporean Chinese men

10.1016/j.orcp.2013.05.002Obesity Research and Clinical Practice83e283 - e29

Supplementary Table S2 from Histone Methyltransferase NSD2 Activates PKCα to Drive Metabolic Reprogramming and Lenalidomide Resistance in Multiple Myeloma

Supplementary Table S2</p

Supplementary Table S1 from Histone Methyltransferase NSD2 Activates PKCα to Drive Metabolic Reprogramming and Lenalidomide Resistance in Multiple Myeloma

Supplementary Table S1</p