<?xml version="1.0"?>
<Articles JournalTitle="Acta Medica Iranica">
  <Article>
    <Journal>
      <PublisherName>Tehran University of Medical Sciences</PublisherName>
      <JournalTitle>Acta Medica Iranica</JournalTitle>
      <Issn>0044-6025</Issn>
      <Volume>43</Volume>
      <Issue>4</Issue>
      <PubDate PubStatus="epublish">
        <Year>2005</Year>
        <Month>08</Month>
        <Day>15</Day>
      </PubDate>
    </Journal>
    <title locale="en_US">PRODUCTION OF A HUMAN RECOMBINANT ANTIBODY AGAINST SEROTYPE A CANDIDA ALBICANS</title>
    <FirstPage>273</FirstPage>
    <LastPage>278</LastPage>
    <AuthorList>
      <Author>
        <FirstName></FirstName>
        <LastName>A A. Jafari</LastName>
        <affiliation locale="en_US"></affiliation>
      </Author>
    </AuthorList>
    <History>
      <PubDate PubStatus="received">
        <Year>2015</Year>
        <Month>09</Month>
        <Day>28</Day>
      </PubDate>
    </History>
    <abstract locale="en_US">After using 3 different generations of antibodies including human and non-human hyperimmune sera, monoclonal antibodies and chimeric antibodies, more recently a newer approach has been developed in which the antibody genes are cloned directly from a patient peripheral B-lymphocytes and expressed in a host like E. coli. In this study the Candida albicans serotype A (NCTC 3153) mannan was purified using a modified Fehling method and used for selection of human recombinant antibody from a C. albicans phage antibody library. After four rounds of affinity selecting (panning), 2 predominant clones were chosen by DNA fingerprinting and ELISA. A 248 amino acid DNA fragment coding for anti-C. albicans mannan scFv was sequenced and cloned in a pBAD-TOPO cloning vector to produce a soluble and phage free antibody. The analysis of antibody sequences by V base Index (DNAPLOT) confirmed the human antibody origin with the VH4 family in V segment of heavy variable chain and VL3 (Lambda 3) in J segment of the light variable chain. This antibody fragment was purified using immobilized metal affinity chromatography and inmmunoblotted as a 31kDa recombinant protein.</abstract>
    <web_url>https://acta.tums.ac.ir/index.php/acta/article/view/3008</web_url>
    <pdf_url>https://acta.tums.ac.ir/index.php/acta/article/download/3008/2989</pdf_url>
  </Article>
</Articles>
