A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity

Identifying the ligands or regions derived from them which parasites use to invade their target cells has proved to be an excellent strategy for identifying targets for vaccine development. Members of the reticulocyte-binding homologue family (P. fRH), including RH5, have been implicated in invasion...

Full description

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:10336/23459
Acceso en línea:
https://doi.org/10.1016/j.vaccine.2011.11.012
https://repository.urosario.edu.co/handle/10336/23459
Palabra clave:
Binding protein
Chloroquine
Malaria vaccine
Membrane protein
Plasmodium falciparum rh5 protein
Trypsin
Unclassified drug
Amino acid analysis
Amino acid sequence
Article
Binding affinity
Binding competition
Blood sampling
Competitive inhibition
Controlled study
Erythrocyte
Female
Hela cell
Human
Human cell
Immunogenicity
Parasitemia
Peptide mapping
Plasmodium falciparum
Polyacrylamide gel electrophoresis
Priority journal
Protein modification
Protein structure
Protein synthesis
Reversed phase high performance liquid chromatography
Sequence analysis
Structure activity relation
Structure analysis
Western blotting
Amino acid sequence
Amino acid substitution
Animals
Aotus trivirgatus
Carrier proteins
Cell adhesion
Erythrocytes
Humans
Molecular sequence data
Mutant proteins
Plasmodium falciparum
Protein binding
Protein conformation
Sequence alignment
Malaria
Peptide
Receptor
Red blood cell
Structure-activity relationship
Vaccine
missense
Mutation
Rights
License
Abierto (Texto Completo)
id EDOCUR2_a32f6b60d9e8e4ea47728289a9f67923
oai_identifier_str oai:repository.urosario.edu.co:10336/23459
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling eca483d3-a229-42c8-8a6d-3b5e6f002e5b-191225589-1453006a5-2ec3-4faf-8e32-a9d7075d519d-179653065-151890881-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-05-26T00:02:13Z2020-05-26T00:02:13Z2012Identifying the ligands or regions derived from them which parasites use to invade their target cells has proved to be an excellent strategy for identifying targets for vaccine development. Members of the reticulocyte-binding homologue family (P. fRH), including RH5, have been implicated in invasion as adhesins binding to specific receptors on erythrocyte surface. The regions mediating P. fRH5-RBC specific interactions have been identified here by fine mapping the whole P. fRH5 protein sequence. These regions, called high activity binding peptides (HABPs), bind to a receptor which is sensitive to trypsin treatment and inhibit merozoite invasion of RBCs by up to 80%, as has been found for HABP 36727. Our results show that a single amino acid change in the HABP 36727 sequence modifies a peptide's 3D structure, thereby resulting in a loss of specific binding to human RBCs and its inhibition ability, while binding to Aotus RBC remains unmodified. Such invasion differences and binding ability produced by replacing a single amino acid in an essential molecule, such as P. fRH5, highlight the inherent difficulties associated with developing a fully effective vaccine against malaria. © 2011 Elsevier Ltd.application/pdfhttps://doi.org/10.1016/j.vaccine.2011.11.0120264410X13588745https://repository.urosario.edu.co/handle/10336/23459eng646No. 3637VaccineVol. 30Vaccine, ISSN:0264410X, 13588745, Vol.30, No.3 (2012); pp. 637-646https://www.scopus.com/inward/record.uri?eid=2-s2.0-84355165243&doi=10.1016%2fj.vaccine.2011.11.012&partnerID=40&md5=6f971355b7b0c5794fe30e9bcdfaa8cfAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBinding proteinChloroquineMalaria vaccineMembrane proteinPlasmodium falciparum rh5 proteinTrypsinUnclassified drugAmino acid analysisAmino acid sequenceArticleBinding affinityBinding competitionBlood samplingCompetitive inhibitionControlled studyErythrocyteFemaleHela cellHumanHuman cellImmunogenicityParasitemiaPeptide mappingPlasmodium falciparumPolyacrylamide gel electrophoresisPriority journalProtein modificationProtein structureProtein synthesisReversed phase high performance liquid chromatographySequence analysisStructure activity relationStructure analysisWestern blottingAmino acid sequenceAmino acid substitutionAnimalsAotus trivirgatusCarrier proteinsCell adhesionErythrocytesHumansMolecular sequence dataMutant proteinsPlasmodium falciparumProtein bindingProtein conformationSequence alignmentMalariaPeptideReceptorRed blood cellStructure-activity relationshipVaccinemissenseMutationA single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activityarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Arévalo-Pinzón, GabrielaCurtidor, HernandoMuñoz, MarinaPatarroyo, Manuel A.Bermudez, AdrianaPatarroyo, Manuel E.ORIGINALA_single_amino_acid_change_in_the_Plasmo.pdfapplication/pdf1377064https://repository.urosario.edu.co/bitstreams/798c4fff-1737-4bb6-9889-cb3122422b4f/downloaded27f8e99008fac9f18e5731aa7ca2a3MD51TEXTA_single_amino_acid_change_in_the_Plasmo.pdf.txtA_single_amino_acid_change_in_the_Plasmo.pdf.txtExtracted texttext/plain57805https://repository.urosario.edu.co/bitstreams/6e00ef6d-e132-41ca-be1f-98b84beab33d/download76b55573b4d4e1ba54b62c9aea2f81caMD52THUMBNAILA_single_amino_acid_change_in_the_Plasmo.pdf.jpgA_single_amino_acid_change_in_the_Plasmo.pdf.jpgGenerated Thumbnailimage/jpeg4815https://repository.urosario.edu.co/bitstreams/bfff7acd-1217-4857-b16f-f88701c7874d/download3486d5ead9060ce890f7c4b7d7a3fb6fMD5310336/23459oai:repository.urosario.edu.co:10336/234592022-05-02 07:37:20.982784https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity
title A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity
spellingShingle A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity
Binding protein
Chloroquine
Malaria vaccine
Membrane protein
Plasmodium falciparum rh5 protein
Trypsin
Unclassified drug
Amino acid analysis
Amino acid sequence
Article
Binding affinity
Binding competition
Blood sampling
Competitive inhibition
Controlled study
Erythrocyte
Female
Hela cell
Human
Human cell
Immunogenicity
Parasitemia
Peptide mapping
Plasmodium falciparum
Polyacrylamide gel electrophoresis
Priority journal
Protein modification
Protein structure
Protein synthesis
Reversed phase high performance liquid chromatography
Sequence analysis
Structure activity relation
Structure analysis
Western blotting
Amino acid sequence
Amino acid substitution
Animals
Aotus trivirgatus
Carrier proteins
Cell adhesion
Erythrocytes
Humans
Molecular sequence data
Mutant proteins
Plasmodium falciparum
Protein binding
Protein conformation
Sequence alignment
Malaria
Peptide
Receptor
Red blood cell
Structure-activity relationship
Vaccine
missense
Mutation
title_short A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity
title_full A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity
title_fullStr A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity
title_full_unstemmed A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity
title_sort A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity
dc.subject.keyword.spa.fl_str_mv Binding protein
Chloroquine
Malaria vaccine
Membrane protein
Plasmodium falciparum rh5 protein
Trypsin
Unclassified drug
Amino acid analysis
Amino acid sequence
Article
Binding affinity
Binding competition
Blood sampling
Competitive inhibition
Controlled study
Erythrocyte
Female
Hela cell
Human
Human cell
Immunogenicity
Parasitemia
Peptide mapping
Plasmodium falciparum
Polyacrylamide gel electrophoresis
Priority journal
Protein modification
Protein structure
Protein synthesis
Reversed phase high performance liquid chromatography
Sequence analysis
Structure activity relation
Structure analysis
Western blotting
Amino acid sequence
Amino acid substitution
Animals
Aotus trivirgatus
Carrier proteins
Cell adhesion
Erythrocytes
Humans
Molecular sequence data
Mutant proteins
Plasmodium falciparum
Protein binding
Protein conformation
Sequence alignment
Malaria
Peptide
Receptor
Red blood cell
Structure-activity relationship
Vaccine
topic Binding protein
Chloroquine
Malaria vaccine
Membrane protein
Plasmodium falciparum rh5 protein
Trypsin
Unclassified drug
Amino acid analysis
Amino acid sequence
Article
Binding affinity
Binding competition
Blood sampling
Competitive inhibition
Controlled study
Erythrocyte
Female
Hela cell
Human
Human cell
Immunogenicity
Parasitemia
Peptide mapping
Plasmodium falciparum
Polyacrylamide gel electrophoresis
Priority journal
Protein modification
Protein structure
Protein synthesis
Reversed phase high performance liquid chromatography
Sequence analysis
Structure activity relation
Structure analysis
Western blotting
Amino acid sequence
Amino acid substitution
Animals
Aotus trivirgatus
Carrier proteins
Cell adhesion
Erythrocytes
Humans
Molecular sequence data
Mutant proteins
Plasmodium falciparum
Protein binding
Protein conformation
Sequence alignment
Malaria
Peptide
Receptor
Red blood cell
Structure-activity relationship
Vaccine
missense
Mutation
dc.subject.keyword.eng.fl_str_mv missense
Mutation
description Identifying the ligands or regions derived from them which parasites use to invade their target cells has proved to be an excellent strategy for identifying targets for vaccine development. Members of the reticulocyte-binding homologue family (P. fRH), including RH5, have been implicated in invasion as adhesins binding to specific receptors on erythrocyte surface. The regions mediating P. fRH5-RBC specific interactions have been identified here by fine mapping the whole P. fRH5 protein sequence. These regions, called high activity binding peptides (HABPs), bind to a receptor which is sensitive to trypsin treatment and inhibit merozoite invasion of RBCs by up to 80%, as has been found for HABP 36727. Our results show that a single amino acid change in the HABP 36727 sequence modifies a peptide's 3D structure, thereby resulting in a loss of specific binding to human RBCs and its inhibition ability, while binding to Aotus RBC remains unmodified. Such invasion differences and binding ability produced by replacing a single amino acid in an essential molecule, such as P. fRH5, highlight the inherent difficulties associated with developing a fully effective vaccine against malaria. © 2011 Elsevier Ltd.
publishDate 2012
dc.date.created.spa.fl_str_mv 2012
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:13Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:13Z
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.vaccine.2011.11.012
dc.identifier.issn.none.fl_str_mv 0264410X
13588745
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23459
url https://doi.org/10.1016/j.vaccine.2011.11.012
https://repository.urosario.edu.co/handle/10336/23459
identifier_str_mv 0264410X
13588745
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 646
dc.relation.citationIssue.none.fl_str_mv No. 3
dc.relation.citationStartPage.none.fl_str_mv 637
dc.relation.citationTitle.none.fl_str_mv Vaccine
dc.relation.citationVolume.none.fl_str_mv Vol. 30
dc.relation.ispartof.spa.fl_str_mv Vaccine, ISSN:0264410X, 13588745, Vol.30, No.3 (2012); pp. 637-646
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-84355165243&doi=10.1016%2fj.vaccine.2011.11.012&partnerID=40&md5=6f971355b7b0c5794fe30e9bcdfaa8cf
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
bitstream.url.fl_str_mv https://repository.urosario.edu.co/bitstreams/798c4fff-1737-4bb6-9889-cb3122422b4f/download
https://repository.urosario.edu.co/bitstreams/6e00ef6d-e132-41ca-be1f-98b84beab33d/download
https://repository.urosario.edu.co/bitstreams/bfff7acd-1217-4857-b16f-f88701c7874d/download
bitstream.checksum.fl_str_mv ed27f8e99008fac9f18e5731aa7ca2a3
76b55573b4d4e1ba54b62c9aea2f81ca
3486d5ead9060ce890f7c4b7d7a3fb6f
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
MD5
repository.name.fl_str_mv Repositorio institucional EdocUR
repository.mail.fl_str_mv edocur@urosario.edu.co
_version_ 1814167464638939136