Protective immunity provided by a new modified SERA protein peptide: Its immunogenetic characteristics and correlation with 3D structure
The serine repeat antigen (SERA) protein is a leading candidate molecule for inclusion as a component in a multi-antigen, multi-stage, minimal subunit-based, chemically synthesised anti-malarial vaccine. Peptides having high red blood cell binding affinity (known as HABPs) have been identified in th...
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2012
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| Acceso en línea: | https://repository.urosario.edu.co/handle/10336/24252 https://doi.org/10.1007/s00726-011-1061-5 |
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ir-10336-242522022-05-02T12:37:14Z Protective immunity provided by a new modified SERA protein peptide: Its immunogenetic characteristics and correlation with 3D structure Bermudez, Adriana Moreno-Vranich, Armando Patarroyo, Manuel E. Malaria vaccine Peptide derivative Serine repeat antigen protein derivative Unclassified drug Amino acid sequence Amino acid substitution Animal experiment Antibody production Article Binding affinity Carboxy terminal sequence Controlled study Erythrocyte Haplorhini Immunity Immunogenicity Malaria falciparum Molecular model Nonhuman Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Three dimensional imaging Amino acid sequence Animals Aotidae Erythrocytes Malaria vaccines Molecular sequence data Plasmodium falciparum Plasmodium falciparum Malaria vaccine Nmr Sera 5 Structure protozoan amino acid falciparum molecular Antigens Malaria Models Repetitive sequences The serine repeat antigen (SERA) protein is a leading candidate molecule for inclusion as a component in a multi-antigen, multi-stage, minimal subunit-based, chemically synthesised anti-malarial vaccine. Peptides having high red blood cell binding affinity (known as HABPs) have been identified in this protein. The 6733 HABP was located in the C-terminal portion of the 47-kDa fragment while HABP 6754 was located in the C-terminal region of the 56-kDa fragment. These conserved HABPs failed to induce an immune response. Critical red blood cell binding residues and/or their neighbours (assessed by glycine-analogue scanning) were replaced by others having the same mass, volume and surface but different polarity, rendering some of them highly immunogenic when assessed by antibody production against the parasite or its proteins and protection-inducers against experimental challenge with a highly infectious Aotus monkey-adapted Plasmodium falciparum strain. This manuscript presents some modified HABPs as vaccine candidate components for enriching our tailor-made anti-malarial vaccine repertoire, as well as their 3D structure obtained by 1H-NMR displaying a short-structured region, differently from the native ones having random structures. © 2011 Springer-Verlag. 2012 2020-05-26T00:10:43Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 09394451 14382199 https://repository.urosario.edu.co/handle/10336/24252 https://doi.org/10.1007/s00726-011-1061-5 eng info:eu-repo/semantics/openAccess application/pdf instname:Universidad del Rosario |
| institution |
EdocUR - Universidad del Rosario |
| collection |
DSpace |
| language |
Inglés (English) |
| topic |
Malaria vaccine Peptide derivative Serine repeat antigen protein derivative Unclassified drug Amino acid sequence Amino acid substitution Animal experiment Antibody production Article Binding affinity Carboxy terminal sequence Controlled study Erythrocyte Haplorhini Immunity Immunogenicity Malaria falciparum Molecular model Nonhuman Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Three dimensional imaging Amino acid sequence Animals Aotidae Erythrocytes Malaria vaccines Molecular sequence data Plasmodium falciparum Plasmodium falciparum Malaria vaccine Nmr Sera 5 Structure protozoan amino acid falciparum molecular Antigens Malaria Models Repetitive sequences |
| spellingShingle |
Malaria vaccine Peptide derivative Serine repeat antigen protein derivative Unclassified drug Amino acid sequence Amino acid substitution Animal experiment Antibody production Article Binding affinity Carboxy terminal sequence Controlled study Erythrocyte Haplorhini Immunity Immunogenicity Malaria falciparum Molecular model Nonhuman Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Three dimensional imaging Amino acid sequence Animals Aotidae Erythrocytes Malaria vaccines Molecular sequence data Plasmodium falciparum Plasmodium falciparum Malaria vaccine Nmr Sera 5 Structure protozoan amino acid falciparum molecular Antigens Malaria Models Repetitive sequences Bermudez, Adriana Moreno-Vranich, Armando Patarroyo, Manuel E. Protective immunity provided by a new modified SERA protein peptide: Its immunogenetic characteristics and correlation with 3D structure |
| description |
The serine repeat antigen (SERA) protein is a leading candidate molecule for inclusion as a component in a multi-antigen, multi-stage, minimal subunit-based, chemically synthesised anti-malarial vaccine. Peptides having high red blood cell binding affinity (known as HABPs) have been identified in this protein. The 6733 HABP was located in the C-terminal portion of the 47-kDa fragment while HABP 6754 was located in the C-terminal region of the 56-kDa fragment. These conserved HABPs failed to induce an immune response. Critical red blood cell binding residues and/or their neighbours (assessed by glycine-analogue scanning) were replaced by others having the same mass, volume and surface but different polarity, rendering some of them highly immunogenic when assessed by antibody production against the parasite or its proteins and protection-inducers against experimental challenge with a highly infectious Aotus monkey-adapted Plasmodium falciparum strain. This manuscript presents some modified HABPs as vaccine candidate components for enriching our tailor-made anti-malarial vaccine repertoire, as well as their 3D structure obtained by 1H-NMR displaying a short-structured region, differently from the native ones having random structures. © 2011 Springer-Verlag. |
| format |
Artículo (Article) |
| author |
Bermudez, Adriana Moreno-Vranich, Armando Patarroyo, Manuel E. |
| author_facet |
Bermudez, Adriana Moreno-Vranich, Armando Patarroyo, Manuel E. |
| author_sort |
Bermudez, Adriana |
| title |
Protective immunity provided by a new modified SERA protein peptide: Its immunogenetic characteristics and correlation with 3D structure |
| title_short |
Protective immunity provided by a new modified SERA protein peptide: Its immunogenetic characteristics and correlation with 3D structure |
| title_full |
Protective immunity provided by a new modified SERA protein peptide: Its immunogenetic characteristics and correlation with 3D structure |
| title_fullStr |
Protective immunity provided by a new modified SERA protein peptide: Its immunogenetic characteristics and correlation with 3D structure |
| title_full_unstemmed |
Protective immunity provided by a new modified SERA protein peptide: Its immunogenetic characteristics and correlation with 3D structure |
| title_sort |
protective immunity provided by a new modified sera protein peptide: its immunogenetic characteristics and correlation with 3d structure |
| publishDate |
2012 |
| url |
https://repository.urosario.edu.co/handle/10336/24252 https://doi.org/10.1007/s00726-011-1061-5 |
| _version_ |
1740173048296767488 |
| score |
12,131701 |