Antibody fragment expression and purification.
Identifieur interne : 001950 ( PubMed/Corpus ); précédent : 001949; suivant : 001951Antibody fragment expression and purification.
Auteurs : Dimana Dimitrova ; Vidita Choudhry ; Christopher C. BroderSource :
- Methods in molecular biology (Clifton, N.J.) [ 1064-3745 ] ; 2009.
English descriptors
- KwdEn :
- MESH :
- chemical , isolation & purification : Immunoglobulin Fab Fragments, Immunoglobulin Fragments.
- chemical , metabolism : Immunoglobulin Fragments.
- methods : Molecular Biology.
- Bacteriophages, Humans.
Abstract
Interest in the potential of monoclonal antibodies (mAbs) to serve as therapeutic agents has surged in the past decade with a major emphasis on human viral diseases. There has been much attention in this area directed towards the human immunodeficiency virus type-1 (HIV-1) and promising research developments have emerged on the inhibition of HIV-1 infection by mAbs and the identification of several highly conserved neutralizing epitopes. More recently, potent fully-human neutralizing mAbs have been developed against a variety of important human viral disease agents including the paramyxoviruses Hendra virus and Nipah virus, and human or humanized mAbs have been developed against severe acute respiratory syndrome coronavirus (SARS CoV), and West Nile virus, among others. Most of these more recently developed antiviral mAbs have come from the use of antibody phage-display technologies and the implementation of simplified, inexpensive yet efficient methods, for expressing and purifying the initially selected fragment antibodies is of prime importance in further facilitating this area of research.
DOI: 10.1007/978-1-59745-554-1_25
PubMed: 19252844
Links to Exploration step
pubmed:19252844Le document en format XML
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<front><div type="abstract" xml:lang="en">Interest in the potential of monoclonal antibodies (mAbs) to serve as therapeutic agents has surged in the past decade with a major emphasis on human viral diseases. There has been much attention in this area directed towards the human immunodeficiency virus type-1 (HIV-1) and promising research developments have emerged on the inhibition of HIV-1 infection by mAbs and the identification of several highly conserved neutralizing epitopes. More recently, potent fully-human neutralizing mAbs have been developed against a variety of important human viral disease agents including the paramyxoviruses Hendra virus and Nipah virus, and human or humanized mAbs have been developed against severe acute respiratory syndrome coronavirus (SARS CoV), and West Nile virus, among others. Most of these more recently developed antiviral mAbs have come from the use of antibody phage-display technologies and the implementation of simplified, inexpensive yet efficient methods, for expressing and purifying the initially selected fragment antibodies is of prime importance in further facilitating this area of research.</div>
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<Abstract><AbstractText>Interest in the potential of monoclonal antibodies (mAbs) to serve as therapeutic agents has surged in the past decade with a major emphasis on human viral diseases. There has been much attention in this area directed towards the human immunodeficiency virus type-1 (HIV-1) and promising research developments have emerged on the inhibition of HIV-1 infection by mAbs and the identification of several highly conserved neutralizing epitopes. More recently, potent fully-human neutralizing mAbs have been developed against a variety of important human viral disease agents including the paramyxoviruses Hendra virus and Nipah virus, and human or humanized mAbs have been developed against severe acute respiratory syndrome coronavirus (SARS CoV), and West Nile virus, among others. Most of these more recently developed antiviral mAbs have come from the use of antibody phage-display technologies and the implementation of simplified, inexpensive yet efficient methods, for expressing and purifying the initially selected fragment antibodies is of prime importance in further facilitating this area of research.</AbstractText>
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<ReferenceList><Reference><Citation>Curr Opin Biotechnol. 1997 Aug;8(4):503-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9265732</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Infect Dis. 1997 Nov;176(5):1215-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9359721</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Immunol. 1997 Apr;9(2):201-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9099794</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Clin Chem. 2005 May;51(5):830-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15718486</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Med. 2005 May;11(5):522-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15852016</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Cancer. 2007 Sep;7(9):701-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17721434</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Expert Rev Anti Infect Ther. 2006 Feb;4(1):57-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16441209</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Appl Environ Microbiol. 2006 Jul;72(7):4589-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16820448</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2007 Jun 20;363(1):79-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17306322</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Oncogene. 2007 May 28;26(25):3714-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17530025</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):12123-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17620608</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Jan;80(2):891-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16378991</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
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