The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
The importance of CSP- and STARP-derived ? and ? dihedral angles in mHABP structure was analysed by 1H NMR in the search for molecules which can be included as components of a first-line-of-defence Plasmodium falciparum sporozoite multi-epitope vaccine against the most lethal form of human malaria....
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2012
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/23512
- Acceso en línea:
- https://doi.org/10.1016/j.bbrc.2012.10.088
https://repository.urosario.edu.co/handle/10336/23512
- Palabra clave:
- Binding protein
Circumsporozoite protein
High activity binding peptide
Major histocompatibility antigen class 2
Proline
Protozoal protein
Sporozoite threonine and asparagine rich protein
Sporozoite vaccine
Unclassified drug
Alpha helix
Amino acid sequence
Article
Complex formation
Hydrogen bond
Immunogenicity
Plasmodium falciparum
Priority journal
Protein structure
Proton nuclear magnetic resonance
Amino acid sequence
Animals
Aotus trivirgatus
Hla-dr beta-chains
Humans
Malaria vaccines
Molecular sequence data
Peptide fragments
Peptides
Plasmodium falciparum
Protozoan proteins
Sporozoites
Plasmodium falciparum
? and ? angles
Antimalarial-vaccine
Hladr?* molecules
Plasmodium falciparum
Pre-erythrocyte stage
secondary
protozoan
biomolecular
Antigens
Nuclear magnetic resonance
Protein structure
- Rights
- License
- Abierto (Texto Completo)
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oai:repository.urosario.edu.co:10336/23512 |
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EDOCUR2 |
network_name_str |
Repositorio EdocUR - U. Rosario |
repository_id_str |
|
spelling |
10ecd4f9-843f-4ef2-bec0-7d39d3381a13-151890881-108b7b42f-4645-4ff5-a2ef-eaccc7f7eab0-12020-05-26T00:02:39Z2020-05-26T00:02:39Z2012The importance of CSP- and STARP-derived ? and ? dihedral angles in mHABP structure was analysed by 1H NMR in the search for molecules which can be included as components of a first-line-of-defence Plasmodium falciparum sporozoite multi-epitope vaccine against the most lethal form of human malaria. Most of the aforementioned dihedral angles were left-hand-like polyproline type II (PPIIL) structures whilst others had right-hand-like ?-helix (?R), thus allowing mHABPS to fit better into MHCII molecules and thereby form an appropriate pMHCII complex and also establish the H-bonds which stabilise such complex and by this means induce an appropriate immune response. This information has great implications for vaccine development, malaria being one of them. © 2012 Elsevier Inc.application/pdfhttps://doi.org/10.1016/j.bbrc.2012.10.0880006291X10902104https://repository.urosario.edu.co/handle/10336/23512eng86No. 4386281Biochemical and Biophysical Research CommunicationsVol. 429Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.429, No.43862 (2012); pp. 81-86https://www.scopus.com/inward/record.uri?eid=2-s2.0-84870391900&doi=10.1016%2fj.bbrc.2012.10.088&partnerID=40&md5=0342f3570a2423c967218557f5ec1927Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBinding proteinCircumsporozoite proteinHigh activity binding peptideMajor histocompatibility antigen class 2ProlineProtozoal proteinSporozoite threonine and asparagine rich proteinSporozoite vaccineUnclassified drugAlpha helixAmino acid sequenceArticleComplex formationHydrogen bondImmunogenicityPlasmodium falciparumPriority journalProtein structureProton nuclear magnetic resonanceAmino acid sequenceAnimalsAotus trivirgatusHla-dr beta-chainsHumansMalaria vaccinesMolecular sequence dataPeptide fragmentsPeptidesPlasmodium falciparumProtozoan proteinsSporozoitesPlasmodium falciparum? and ? anglesAntimalarial-vaccineHladr?* moleculesPlasmodium falciparumPre-erythrocyte stagesecondaryprotozoanbiomolecularAntigensNuclear magnetic resonanceProtein structureThe high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) anglesarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Patarroyo, Manuel E.Bermudez, AdrianaAlba, Martha P.10336/23512oai:repository.urosario.edu.co:10336/235122022-05-02 07:37:21.014655https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co |
dc.title.spa.fl_str_mv |
The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles |
title |
The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles |
spellingShingle |
The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles Binding protein Circumsporozoite protein High activity binding peptide Major histocompatibility antigen class 2 Proline Protozoal protein Sporozoite threonine and asparagine rich protein Sporozoite vaccine Unclassified drug Alpha helix Amino acid sequence Article Complex formation Hydrogen bond Immunogenicity Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Amino acid sequence Animals Aotus trivirgatus Hla-dr beta-chains Humans Malaria vaccines Molecular sequence data Peptide fragments Peptides Plasmodium falciparum Protozoan proteins Sporozoites Plasmodium falciparum ? and ? angles Antimalarial-vaccine Hladr?* molecules Plasmodium falciparum Pre-erythrocyte stage secondary protozoan biomolecular Antigens Nuclear magnetic resonance Protein structure |
title_short |
The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles |
title_full |
The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles |
title_fullStr |
The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles |
title_full_unstemmed |
The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles |
title_sort |
The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles |
dc.subject.keyword.spa.fl_str_mv |
Binding protein Circumsporozoite protein High activity binding peptide Major histocompatibility antigen class 2 Proline Protozoal protein Sporozoite threonine and asparagine rich protein Sporozoite vaccine Unclassified drug Alpha helix Amino acid sequence Article Complex formation Hydrogen bond Immunogenicity Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Amino acid sequence Animals Aotus trivirgatus Hla-dr beta-chains Humans Malaria vaccines Molecular sequence data Peptide fragments Peptides Plasmodium falciparum Protozoan proteins Sporozoites Plasmodium falciparum ? and ? angles Antimalarial-vaccine Hladr?* molecules Plasmodium falciparum Pre-erythrocyte stage |
topic |
Binding protein Circumsporozoite protein High activity binding peptide Major histocompatibility antigen class 2 Proline Protozoal protein Sporozoite threonine and asparagine rich protein Sporozoite vaccine Unclassified drug Alpha helix Amino acid sequence Article Complex formation Hydrogen bond Immunogenicity Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Amino acid sequence Animals Aotus trivirgatus Hla-dr beta-chains Humans Malaria vaccines Molecular sequence data Peptide fragments Peptides Plasmodium falciparum Protozoan proteins Sporozoites Plasmodium falciparum ? and ? angles Antimalarial-vaccine Hladr?* molecules Plasmodium falciparum Pre-erythrocyte stage secondary protozoan biomolecular Antigens Nuclear magnetic resonance Protein structure |
dc.subject.keyword.eng.fl_str_mv |
secondary protozoan biomolecular Antigens Nuclear magnetic resonance Protein structure |
description |
The importance of CSP- and STARP-derived ? and ? dihedral angles in mHABP structure was analysed by 1H NMR in the search for molecules which can be included as components of a first-line-of-defence Plasmodium falciparum sporozoite multi-epitope vaccine against the most lethal form of human malaria. Most of the aforementioned dihedral angles were left-hand-like polyproline type II (PPIIL) structures whilst others had right-hand-like ?-helix (?R), thus allowing mHABPS to fit better into MHCII molecules and thereby form an appropriate pMHCII complex and also establish the H-bonds which stabilise such complex and by this means induce an appropriate immune response. This information has great implications for vaccine development, malaria being one of them. © 2012 Elsevier Inc. |
publishDate |
2012 |
dc.date.created.spa.fl_str_mv |
2012 |
dc.date.accessioned.none.fl_str_mv |
2020-05-26T00:02:39Z |
dc.date.available.none.fl_str_mv |
2020-05-26T00:02:39Z |
dc.type.eng.fl_str_mv |
article |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.coar.fl_str_mv |
http://purl.org/coar/resource_type/c_6501 |
dc.type.spa.spa.fl_str_mv |
Artículo |
dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1016/j.bbrc.2012.10.088 |
dc.identifier.issn.none.fl_str_mv |
0006291X 10902104 |
dc.identifier.uri.none.fl_str_mv |
https://repository.urosario.edu.co/handle/10336/23512 |
url |
https://doi.org/10.1016/j.bbrc.2012.10.088 https://repository.urosario.edu.co/handle/10336/23512 |
identifier_str_mv |
0006291X 10902104 |
dc.language.iso.spa.fl_str_mv |
eng |
language |
eng |
dc.relation.citationEndPage.none.fl_str_mv |
86 |
dc.relation.citationIssue.none.fl_str_mv |
No. 43862 |
dc.relation.citationStartPage.none.fl_str_mv |
81 |
dc.relation.citationTitle.none.fl_str_mv |
Biochemical and Biophysical Research Communications |
dc.relation.citationVolume.none.fl_str_mv |
Vol. 429 |
dc.relation.ispartof.spa.fl_str_mv |
Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.429, No.43862 (2012); pp. 81-86 |
dc.relation.uri.spa.fl_str_mv |
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84870391900&doi=10.1016%2fj.bbrc.2012.10.088&partnerID=40&md5=0342f3570a2423c967218557f5ec1927 |
dc.rights.coar.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
dc.rights.acceso.spa.fl_str_mv |
Abierto (Texto Completo) |
rights_invalid_str_mv |
Abierto (Texto Completo) http://purl.org/coar/access_right/c_abf2 |
dc.format.mimetype.none.fl_str_mv |
application/pdf |
institution |
Universidad del Rosario |
dc.source.instname.spa.fl_str_mv |
instname:Universidad del Rosario |
dc.source.reponame.spa.fl_str_mv |
reponame:Repositorio Institucional EdocUR |
repository.name.fl_str_mv |
Repositorio institucional EdocUR |
repository.mail.fl_str_mv |
edocur@urosario.edu.co |
_version_ |
1814167489273135104 |