Chimeric Synthetic Peptides Containing Two Immunodominant Epitopes from the Envelope gp46 and the Transmembrane gp21 Glycoproteins of HTLV-I Virus

2001 ◽  
Vol 289 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Milenen Hernández Marin ◽  
Patricia Castellanos Pentón ◽  
Yadaris Márquez Bocalandro ◽  
Lilliam Pozo Peña ◽  
Janet Díaz Navarro ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Immunodominant Epitopes ◽  
Envelope Gp46

Silencing of immunodominant epitopes by contiguous sequences in complex synthetic peptides

1992 ◽  
Vol 143 (2) ◽  
pp. 284-297 ◽  
Author(s):  
Yunsheng Wang ◽  
John A. Smith ◽  
Thomas Kamradt ◽  
Malcolm L. Gefter ◽  
David L. Perkins
Keyword(s):  
Synthetic Peptides ◽  
Immunodominant Epitopes

Chimeric Synthetic Peptides from the Envelope (gp46) and the Transmembrane (gp21) Glycoproteins for the Detection of Antibodies to Human T-Cell Leukemia Virus Type II

2001 ◽  
Vol 289 (1) ◽  
pp. 7-12 ◽  
Author(s):  
Milenen Hernández Marin ◽  
Patricia Castellanos Pentón ◽  
Yadaris Márquez Bocalandro ◽  
Lilliam Pozo Peña ◽  
Janet Díaz Navarro ◽  
...  
Keyword(s):  
T Cell ◽  
Virus Type ◽  
Synthetic Peptides ◽  
Leukemia Virus ◽  
Type Ii ◽  
Cell Leukemia ◽  
Cell Leukemia Virus Type ◽  
Human T Cell ◽  
T Cell Leukemia Virus ◽  
Envelope Gp46

scholarly journals Peptide-Based Antibody Detection for Tuberculosis Diagnosis

2008 ◽  
Vol 16 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Guomiao Shen ◽  
Digambar Behera ◽  
Manpreet Bhalla ◽  
Arthur Nadas ◽  
Suman Laal
Keyword(s):  
Control Strategy ◽  
Synthetic Peptide ◽  
Synthetic Peptides ◽  
Diagnostic Methods ◽  
Antibody Detection ◽  
High Quality ◽  
Tb Control ◽  
Tuberculosis Diagnosis ◽  
Immunogenic Proteins ◽  
Immunodominant Epitopes

ABSTRACT Tuberculosis (TB) is a major cause of morbidity and mortality, especially in developing countries. Despite significant limitations, microscopy remains the cornerstone of the global TB control strategy. As the TB epidemic escalates, new diagnostic methods that are accurate and also economical and simple to manufacture and deploy are urgently needed. Although several promising antigens have been identified and evaluated in recent years, the reproducible production of high-quality recombinant mycobacterial proteins with minimal batch-to-batch variation is difficult, laborious, and expensive. To determine the feasibility of devising a synthetic peptide-based diagnostic test for TB, we have delineated the immunodominant epitopes of three candidate antigens, Ag85B, BfrB, and TrxC, that were previously identified to be immunogenic in TB patients. The results demonstrate that combinations of carefully selected synthetic peptides derived from highly immunogenic proteins can be the basis for devising an immunodiagnostic test for TB.

Mapping of Immunodominant Epitopes of the HIV-1 and HIV-2 Integrase Proteins by Recombinant Proteins and Synthetic Peptides

1992 ◽  
Vol 8 (7) ◽  
pp. 1301-1310 ◽  
Author(s):  
CRISTINA VINGA-MARTINS ◽  
THOMAS SCHNEIDER ◽  
ANJA WERNO ◽  
WOLFGANG ROENSPECK ◽  
GEORG PAULI ◽  
...  
Keyword(s):  
Recombinant Proteins ◽  
Synthetic Peptides ◽  
Hiv 1 ◽  
Immunodominant Epitopes

Ristocetin and Botrocetin Involve Two Distinct Domains of von Willebrand Factor for Binding to Platelet Membrane Glycoprotein lb

1990 ◽  
Vol 64 (02) ◽  
pp. 326-332 ◽  
Author(s):  
J P Girma ◽  
Y Takahashi ◽  
A Yoshioka ◽  
J Diaz ◽  
D Meyer
Keyword(s):  
Von Willebrand Factor ◽  
Synthetic Peptides ◽  
Competitive Inhibition ◽  
Final Concentration ◽  
Binding Domain ◽  
Platelet Membrane ◽  
Platelet Glycoprotein ◽  
Membrane Glycoprotein ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryWe have evidence that ristocetin and botrocetin mediate binding of von Willebrand Factor (vWF) to platelet glycoprotein lb (GPIb) through two distinct domains on the vWF molecule. This was established by using monoclonal antibodies (MAbs) to vWF and synthetic peptides derived from the sequence of vWF. MAb 322 and MAb NMC/vW 4 both recognize native vWF as well as fragments containing the GPIb-binding domain of vWF, obtained with the following enzymes: trypsin (116 kDa), V-8 pro tease (Spill, 320 kDa) and V-8 protease plus subtilisin (33-28 kDa). Nevertheless, the lack of reciprocal displacement between the two MAbs in experiments of competitive inhibition for binding to vWF demonstrate that their respective epitopes are separate. Both MAbs inhibit 125I-vWF binding to platelet membrane GPIb and vWF-dependent platelet agglutination induced by ristocetin. However, only MAb NMC/vW4 inhibits these functions in the presence of botrocetin and when ristocetin-induced platelet agglutination is inhibited by MAb 322, botrocetin is still able to restore the agglutination. The involvement of two distinct domains of vWF for binding to GPIb in the presence of ristocetin or botrocetin was confirmed in experiments of binding of 125I-vWF to platelets using as competitor synthetic peptides corresponding to the GPIb binding domain of vWF (Cys 474 to Pro 488 and Ser 692 to Pro 708). At a final concentration of 2.5 mM both peptides inhibit more than 90% of the binding of vWF to ristocetin-treated platelets but are unable to modify this binding in the presence of botrocetin. In conclusion our data suggest that botrocetin and ristocetin involve distinct sites on vWF for binding to GPIb.

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