Introduction. Several studies have been conducted on the use of Immunoglobulin Y (IgY) technology in the fields of diagnostics and therapeutics. IgY is the avian counterpart of the mammalian immunoglobulin G (IgG) which is exclusively transferred from the hen to the yolk thus conferring passive immunization to the growing embryo. However, despite the advantages it offers over the use of mammalian immunoglobulin, IgY technology has remained underutilized. Objective. The objective of this study is to produce an IgY with activity against synthetic peptide analogs of known immunogenic epitopes of the Hepatitis B Surface Antigen (HBsAg) - a molecular marker of Hepatitis B infection. Methods. Chickens were immunized with synthetic peptide analogs of previously reported immunogenic epitopes of the S and the pre-S1 regions of the Hepatitis B surface antigen (HBsAg). IgY specific for the synthetic peptides was isolated by delipidation and salt precipitation and was further purified by affinity chromatography. Purity and molecular weights of the whole IgY molecule and its subunits were assessed and determined by SDS-PAGE. Anti-peptide activity and specificity were determined by indirect ELISA. The study was approved by the Ethical Review Board (ERB) and Technical Review Board of the Research Implementation and Development Office (RIDO), University of the Philippines Manila. Results and Conclusion. The IgY that was purified in this study had an approximate molecular weight of 165 kilodaltons. The heavy and light chains are 60 and 28 kilodaltons, respectively. The affinity purified IgY demonstrated anti-peptide antibody activity against synthetic peptide analogs of known immunogenic epitopes of the HBsAg. Specific binding against a battery of synthetic peptides also revealed that the affinity purified IgY specifically binds to the known immunogenic epitope of the HBsAg.
HEPATITIS B SURFACE ANTIGENS ; HEPATITIS B ANTIGENS ; HEPATITIS B VIRUS ; IGY

Objective: To identify unique immunogenic epitopes of Zika virus non-structural 1 (NS1) antigen and produce immunoglobulin Y (IgY) for potential use in he diagnosis of of Zika virus infection. Methods: Immunogenic epitopes were identified using in silico B-cell epitope prediction. A synthetic peptide analog of the predicted epitope was used to induce antipeptide IgY production in hens which was purified using affinity chromatography. Presence of purified IgY and its binding specificity were performed by gel electrophoresis and ELISA, respectively. Results: Out of the nine continuous epitopes identified, the sequence at position 193-208 (LKVREDYSLECDPAVI) was selected and used to produce anti-peptide IgY. The produced IgY was found to bind to the synthetic analog of the Zika virus NS1 immunogenic epitope but not to other flaviviruses and random peptides from other pathogens. Conclusions: In this study, we identified an immunogenic epitope unique to Zika virus that can be used to develop a serodiagnostic tool that specifically detect Zika virus infection.

This article describes the partnership between the College of Public Health, University of the Philippines Manila and the province of Laguna in the context of implementation of the field practice course. This partnership paved the way for the development and implementation of projects in seven field practice sites. Projects concentrated mainly on improving quality of data and health information system, development of educational materials, and addressing health problems such as tuberculosis, hypertension and rabies. After the implementation of the various activities, there is a need for both parties (the College of Public Health and the Provincial Health Office of Laguna) to monitor and evaluate if projects have been sustained. Moreover, successful projects must also be fully documented which can serve as models for other areas in the province of Laguna.

Human ; Rabies ; Health Information Systems ; Public Health ; Tuberculosis ; Quality Improvement ; Universities ; Teaching Materials ; Hypertension

Spider venoms and toxins are valuable sources of lead compounds for drug development due to their essential role in cellular and physiological processes targeting various receptors. Here, we present the protein profile of the venom of Phlogiellus bundokalbo, an endemic Philippine tarantula, to screen and characterize its cytotoxicity against MCF-7 cells, secretory phospholipase a2 (sPLA2), and neurotoxicity to evaluate its potential anticancer properties. Spider venom was extracted via electrical stimulation. Venom components were fractionated by reversed-phase high-performance liquid chromatography and characterized through liquid chromatography-mass spectrometry (LC-MS) and SDS-PAGE analysis before assay. The resulting five venom fractions were amphiphilic peptides showing cytotoxicity against MCF-7 cells in a concentrationdependent manner (IC50 ranging from 52.25μg/ml to 110.20μg/ml) after 24-hour incubation. Cells appeared detached, rounded, and shrunk with cytoplasmic condensation upon overnight incubation with venom fractions. The sPLA2 was observed in all the venom fractions tested for cytotoxicity. Venom fractions revealed a predominant mass of ~3-5 kDa with LC-MS analysis. Results showed distinct similar mass as μ- theraphotoxin-Phlo1a, an Australian tarantula, Phlogiellus sp. toxin with inhibitor cystine knot motif. The venom fractions exhibit excitatory neurotoxins that might activate presynaptic voltage-gated ion channels, such as an agonist or gating modifier toxins that slow down the channel inactivation similar to spider toxins. In conclusion, the spider venom of P. bundokalbo exhibits cytotoxic, phospholipase A2, and neuroactive properties suggesting that its venom components, upon further purification and structure-function analysis, can be potential tools in the development of targeted breast chemotherapeutics.
Spider Venoms ; Phospholipases