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....

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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)
id EDOCUR2_3937705eabfcfd3acf87d9f174c98817
oai_identifier_str oai:repository.urosario.edu.co:10336/23512
network_acronym_str 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
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