Document Detail


The binding affinity of double-stranded RNA motifs to HIV-1 Tat protein affects transactivation and the neutralizing capacity of anti-Tat antibodies elicited after intranasal immunization.
MedLine Citation:
PMID:  15789358     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In this study we examined the hypothesis that the binding affinity of two double-stranded (ds) RNA motifs to HIV-1 Tat protein might affect transactivation and the type of anti-Tat immune responses. Using surface plasmon resonance technology we demonstrated the capacity of the poly(A):poly(U) (pA:pU) motif to bind with high affinity to a totally synthetic Tat protein and to inhibit more efficiently the Tat/transactivation response element (TAR) RNA interaction as compared to the poly(I):poly(C) (pI:pC) motif. Furthermore, the pA:pU motif was tenfold more effective in inhibiting Tat-driven transactivation than the pI:pC motif. Following intranasal immunization of mice, both dsRNA motifs enhanced the antibody (serum and mucosal) and cellular responses to Tat. However, only the serum samples of mice immunized with Tat + pI:pC inhibited Tat-driven transactivation. The profile of serum antibody subclasses together with the secreted cytokines by Tat-stimulated splenocyte cultures indicated that both dsRNA motifs favored the induction of a balanced Th1 and Th2 immune response. The demonstration in this study that two dsRNA motifs had a marked effect on Tat/TAR RNA interaction and on the neutralizing capacity of anti-Tat specific antibody responses highlights their potential for biological applications and the importance of selecting the appropriate motif as an adjuvant for vaccine design.
Authors:
Charalambos D Partidos; Johan Hoebeke; Emmanuel Moreau; Olivier Chaloin; Mélanie Tunis; Guillaume Belliard; Jean-Paul Briand; Claude Desgranges; Sylviane Muller
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of immunology     Volume:  35     ISSN:  0014-2980     ISO Abbreviation:  Eur. J. Immunol.     Publication Date:  2005 May 
Date Detail:
Created Date:  2005-05-02     Completed Date:  2005-06-28     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  1273201     Medline TA:  Eur J Immunol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  1521-9     Citation Subset:  IM    
Affiliation:
UPR 9021, Institut de Biologie Moléculaire et Cellulaire, CNRS, Strasbourg, France. H.Partidos@ibmc.u-strasbg.fr
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MeSH Terms
Descriptor/Qualifier:
Administration, Intranasal
Animals
Antibody Specificity / immunology
Enzyme-Linked Immunosorbent Assay
Female
Gene Products, tat / immunology,  metabolism*
HIV-1 / immunology,  metabolism*
Interferon-gamma / immunology
Interleukin-2 / immunology
Mice
Mice, Inbred BALB C
RNA, Double-Stranded / administration & dosage,  immunology*,  metabolism*
RNA, Viral / administration & dosage,  immunology,  metabolism
Surface Plasmon Resonance
T-Lymphocytes / immunology
Transcriptional Activation*
tat Gene Products, Human Immunodeficiency Virus
Chemical
Reg. No./Substance:
0/Gene Products, tat; 0/Interleukin-2; 0/RNA, Double-Stranded; 0/RNA, Viral; 0/tat Gene Products, Human Immunodeficiency Virus; 82115-62-6/Interferon-gamma

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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