<?xml version="1.0" encoding="UTF-8"?>
<article>
    <title>Functional analysis of the L Protein of Nipah Virus Using Minigenome System</title>
    <authors>
        <author>Ali Shahandeh</author><author>Amir Bin Rabu</author>
    </authors>
    <affiliations>
        <affiliation>School of Biosciences and Biotechnology, Faculty of Science and Technology, University Kebangsaan Malaysia (UKM), 43600, Bangi, Selangor, Malaysia</affiliation>
    </affiliations>
    <emails>
        <email>a.shahandeh@gmail.com</email><email>amirrabu@gmail.com</email>
    </emails>
    <journal>
        <name>International Journal of Fundamental Physical Sciences (IJFPS)</name>
        <volume>3</volume>
        <issue>3</issue>
        <pages>36-42</pages>
        <date>September, 2013</date>
        <issn>2231-8186</issn>
        <doi>https://doi.org/10.14331/ijfps.2013.330052</doi>
    </journal>
    <abstract>Nipah virus (NiV) was identified in Malaysia in 1998 as the etiological agent of an outbreak of acute encephalitis with high mortality. The L gene of NiV encodes the RNA-dependent RNA polymerase required for replication. This study investigates the role of the N-terminal domain of the L protein through deletion mutagenesis and a minigenome assay system. Five N-terminal deletions were introduced and tested for function using a minigenome system encoding a CAT reporter. Results show that the first 100 amino acids of the L protein are essential for transcription and possibly phosphoprotein interaction. These findings highlight the importance of the NH2-terminal domain in transcription and provide a foundation for antiviral strategies targeting this domain.</abstract>
    <keywords>L gene, polymerase protein, mutagenesis, Nipah virus</keywords>
    <license>https://creativecommons.org/licenses/by/4.0/</license>
</article>
