IMMUNOGENICITY AND PROTECTIVE EFFICACY OF RECOMBINANT VACCINE BASED ON THE RECEPTOR-BINDING DOMAIN OF THE PLASMODIUM VIVAX DUFFY BINDING PROTEIN IN AOTUS MONKEYS

2005 ◽  
Vol 73 (5_suppl) ◽  
pp. 25-31 ◽  
Author(s):  
MYRIAM ARÉVALO-HERRERA ◽  
ROSALIE DOMINIK ◽  
SÓCRATES HERRERA ◽  
CHETAN E. CHITNIS ◽  
SYED S. YAZDANI ◽  
...  
Keyword(s):  
Plasmodium Vivax ◽  
Receptor Binding ◽  
Protective Efficacy ◽  
Binding Protein ◽  
Recombinant Vaccine ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Duffy Binding Protein

scholarly journals In-silico design of a multi-epitope recombinant vaccine against SARS-CoV-2 targeting the receptor binding domain

2020 ◽  
Author(s):  
Harshawardhan Pande
Keyword(s):  
T Cell ◽  
B Cell ◽  
Receptor Binding ◽  
In Silico ◽  
Neutralizing Antibodies ◽  
De Novo ◽  
Recombinant Vaccine ◽  
Binding Domain ◽  
Surface Glycoprotein ◽  
Receptor Binding Domain

The COVID-19 pandemic caused by the SARS-CoV-2 virus is posing a major global challenge due to its rapid infectivity and lethality. Despite a global effort towards creating a vaccine, no viable vaccine currently exists. While multiple bioinformatic studies have attempted to predict epitopes, they have focused on the whole spike protein without considering antibody mediated enhancement or Th-2 immunopathology and have missed some important but less antigenic epitopes in the receptor binding domain. Therefore, this study used in silico methods to design and evaluate a potential multiepitope vaccine that specifically targets the receptor binding domain due to its critical function in viral entry. Immunoinformatic tools were used to specifically examine the receptor binding domain of the surface glycoprotein for suitable T cell and B cell epitopes. The selected 5 B cell and 8 T cell epitopes were then constructed into a subunit vaccine and appropriate adjuvants along with the universal immunogenic PADRE sequence were added to boost efficacy. The structure of the vaccine construct was predicted through a de novo approach and molecular docking simulations were performed which demonstrated high affinity binding to TLR 5 receptor and appropriate HLA proteins. Finally, the vaccine candidate was cloned into an expression vector for use as a recombinant vaccine. Similarities to some recent epitope mapping studies suggest a high potential for eliciting neutralizing antibodies and generating a favorable overall immune response.

scholarly journals Biochemical, Biophysical, and Functional Characterization of Bacterially Expressed and Refolded Receptor Binding Domain ofPlasmodium vivaxDuffy-binding Protein

2001 ◽  
Vol 276 (20) ◽  
pp. 17111-17116 ◽  
Author(s):  
Sanjay Singh ◽  
Kailash Pandey ◽  
Rana Chattopadhayay ◽  
Syed Shams Yazdani ◽  
Andrew Lynn ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Protein ◽  
Functional Characterization ◽  
Binding Domain ◽  
Receptor Binding Domain

Immunogenicity and Protective Efficacy of a Highly Thermotolerant, Trimeric SARS-CoV-2 Receptor Binding Domain Derivative

2021 ◽  
Author(s):  
Sameer Kumar Malladi ◽  
Unnatiben Rajeshbhai Patel ◽  
Raju S. Rajmani ◽  
Randhir Singh ◽  
Suman Pandey ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Protective Efficacy ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Domain Derivative

Genetic polymorphism of the Duffy receptor binding domain of Plasmodium vivax in Colombian wild isolates

1996 ◽  
Vol 78 (1-2) ◽  
pp. 269-272 ◽  
Author(s):  
Elizabeth Ampudia ◽  
Manuel Alfonso Patarroyo ◽  
Manuel Elkin Patarroyo ◽  
Luis Angel Murillo
Keyword(s):  
Genetic Polymorphism ◽  
Plasmodium Vivax ◽  
Receptor Binding ◽  
Binding Domain ◽  
Receptor Binding Domain

The analysis of Plasmodium vivax Duffy receptor binding domain gene sequence from resurgent Korea isolates

2001 ◽  
Vol 87 (12) ◽  
pp. 1007-1010 ◽  
Author(s):  
In Suh ◽  
Kenneth J. Hoffman ◽  
Sang-Hyun Kim ◽  
Ki-Joon Song ◽  
Jin-Won Song ◽  
...  
Keyword(s):  
Plasmodium Vivax ◽  
Receptor Binding ◽  
Gene Sequence ◽  
Binding Domain ◽  
Receptor Binding Domain

Destabilizing the Structural Integrity of SARS-CoV2 Receptor Proteins by Curcumin Along with Hydroxychloroquine: An Insilco Approach for a Combination Therapy

2020 ◽  
Author(s):  
Akhileshwar Srivastava ◽  
Divya Singh
Keyword(s):  
Binding Energy ◽  
Combination Therapy ◽  
Receptor Binding ◽  
Structural Integrity ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Receptor Proteins ◽  
Main Protease ◽  
The Stability ◽  
Therapeutic Activities

Presently, an emerging disease (COVID-19) has been spreading across the world due to coronavirus (SARS-CoV2). For treatment of SARS-CoV2 infection, currently hydroxychloroquine has been suggested by researchers, but it has not been found enough effective against this virus. The present study based on in silico approaches was designed to enhance the therapeutic activities of hydroxychloroquine by using curcumin as an adjunct drug against SARS-CoV2 receptor proteins: main-protease and S1 receptor binding domain (RBD). The webserver (ANCHOR) showed the higher protein stability for both receptors with disordered score (<0.5). The molecular docking analysis revealed that the binding energy (-24.58 kcal/mol) of hydroxychloroquine was higher than curcumin (-20.47 kcal/mol) for receptor main-protease, whereas binding energy of curcumin (<a>-38.84</a> kcal/mol) had greater than hydroxychloroquine<a> (-35.87</a> kcal/mol) in case of S1 receptor binding domain. Therefore, this study suggested that the curcumin could be used as combination therapy along with hydroxychloroquine for disrupting the stability of SARS-CoV2 receptor proteins

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