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High level expression, purification and characterization of recombinant CCR5 as a vaccine candidate against HIV.
- Source :
-
Protein expression and purification [Protein Expr Purif] 2013 Jun; Vol. 89 (2), pp. 124-30. Date of Electronic Publication: 2013 Mar 29. - Publication Year :
- 2013
-
Abstract
- Cysteine-cysteine chemokine receptor type 5 (CCR5) is an important co-receptor for human immunodeficiency virus (HIV) infection and CCR5 neutralizing agents have proven efficient in patients suffering from HIV infection. Here, we expressed and purified various CCR5 vaccines named rCCR5, PADRE-rCCR5, GST-C1 and GST-C2 composed of different epitopes of CCR5. Results showed that vaccines containing multiple epitopes (rCCR5 and PADRE-rCCR5) induced stronger immune responses than single-epitope ones (GST-C1 and GST-C2). In addition, the elicited antibodies can specifically bind CCR5(+) U937 but not CCR5(-) Wish cells. These results demonstrate that the CCR5 vaccines are useful for further research, especially for the in vitro preclinical evaluation of their potential as biological CCR5 neutralizing agents.<br /> (Copyright © 2013 Elsevier Inc. All rights reserved.)
- Subjects :
- AIDS Vaccines chemistry
AIDS Vaccines immunology
Amino Acid Sequence
Animals
Antibody Formation
BALB 3T3 Cells
Base Sequence
Cell Line
Cloning, Molecular
Epitopes chemistry
Epitopes genetics
Epitopes immunology
Epitopes therapeutic use
Escherichia coli genetics
HIV Infections immunology
Humans
Mice
Molecular Sequence Data
Plasmids genetics
Receptors, CCR5 chemistry
Receptors, CCR5 immunology
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins immunology
Recombinant Proteins therapeutic use
AIDS Vaccines genetics
AIDS Vaccines therapeutic use
HIV Infections prevention & control
HIV-1 immunology
Receptors, CCR5 genetics
Receptors, CCR5 therapeutic use
Subjects
Details
- Language :
- English
- ISSN :
- 1096-0279
- Volume :
- 89
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Protein expression and purification
- Publication Type :
- Academic Journal
- Accession number :
- 23542826
- Full Text :
- https://doi.org/10.1016/j.pep.2013.03.008