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Selection of Intracellular Single-Domain Antibodies Targeting the HIV-1 Vpr Protein by Cytoplasmic Yeast Two-Hybrid System
- Source :
- PLoS ONE, PLoS ONE, 2014, 9 (12), pp.e113729. ⟨10.1371/journal.pone.0113729⟩, PLoS ONE, Public Library of Science, 2014, 9 (e113729 ), <10.1371/journal.pone.0113729>, PLoS ONE, Public Library of Science, 2014, 9 (12), pp.e113729. ⟨10.1371/journal.pone.0113729⟩, PLoS ONE, Vol 9, Iss 12, p e113729 (2014), PLoS ONE, Public Library of Science, 2014, 9 (12), pp.e113729. 〈10.1371/journal.pone.0113729〉
- Publication Year :
- 2014
- Publisher :
- HAL CCSD, 2014.
-
Abstract
- International audience; The targeting of HIV-1 using antibodies is of high interest as molecular tools to better understand the biology of the virus or as a first step toward the design of new inhibitors targeting critical viral intracellular proteins. Small and highly stable llama-derived single-domain antibodies can often be functionally expressed as intracellular antibodies in the cytoplasm of eukaryotic cells. Using a selection method based on the Sos Recruitment System, a cytoplasmic yeast two-hybrid approach, we have isolated single-domain antibodies able to bind HIV-1 Vpr and Capside proteins in the yeast cytoplasm. One anti-Vpr single domain antibody was able to bind the HIV-1 regulatory Vpr protein in the cytoplasm of eukaryotic cells, leading to its delocalization from the nucleus to the cytoplasm. To our knowledge, this is the first description of a functional single-domain intrabody targeting HIV-1 Vpr, isolated using an in vivo cytoplasmic selection method that alleviates some limitations of the conventional yeast two-hybrid system.
- Subjects :
- HIV drug discovery
Cytoplasm
Phage display
viruses
Drug research and development
Plasma protein binding
Protein Engineering
Biochemistry
Intrabody
Antibody Engineering
Immunodeficiency Viruses
Antibody Specificity
BINDING
Macromolecular Engineering
PHAGE DISPLAY
FRAGMENT
Immune System Proteins
Multidisciplinary
biology
Drug discovery
virus diseases
vpr Gene Products, Human Immunodeficiency Virus
Transfection
3. Good health
Cell biology
Medical Microbiology
Viral Pathogens
Medicine
Research Article
Biotechnology
Protein Binding
Science
Two-hybrid screening
Immunology
Saccharomyces cerevisiae
ANTIGEN
Bioengineering
Research and Analysis Methods
Microbiology
Antibodies
Antibody Therapy
Two-Hybrid System Techniques
[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Humans
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Molecular Biology Techniques
[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Molecular Biology
Microbial Pathogens
[SDV.BC] Life Sciences [q-bio]/Cellular Biology
Antibody Cloning
Medicine and health sciences
Pharmacology
Cell Nucleus
INTRABODIES
Biology and Life Sciences
Proteins
HIV
IN-VITRO
Single-Domain Antibodies
biology.organism_classification
Molecular biology
LIFE-CYCLE
Single-domain antibody
Synthetic Bioengineering
REPLICATION
HIV-1
biology.protein
Clinical Immunology
INHIBITORS
MATRIX
Cloning
HeLa Cells
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Database :
- OpenAIRE
- Journal :
- PLoS ONE, PLoS ONE, 2014, 9 (12), pp.e113729. ⟨10.1371/journal.pone.0113729⟩, PLoS ONE, Public Library of Science, 2014, 9 (e113729 ), <10.1371/journal.pone.0113729>, PLoS ONE, Public Library of Science, 2014, 9 (12), pp.e113729. ⟨10.1371/journal.pone.0113729⟩, PLoS ONE, Vol 9, Iss 12, p e113729 (2014), PLoS ONE, Public Library of Science, 2014, 9 (12), pp.e113729. 〈10.1371/journal.pone.0113729〉
- Accession number :
- edsair.doi.dedup.....23824dad671e6404d6233a550da793dd