TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria

Fully-protective, long-lasting, immunological (FPLLI) memory against Plasmodium falciparum malaria regarding immune protection-inducing protein structures (IMPIPS) vaccinated into monkeys previously challenged and re-challenged 60 days later with a lethal Aotus monkey-adapted P. falciparum strain wa...

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Autores:
Tipo de recurso:
Fecha de publicación:
2016
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23515
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2016.06.115
https://repository.urosario.edu.co/handle/10336/23515
Palabra clave:
Binding protein
Hla dr antigen
Hla drb3 antigen
Hla drb4 antigen
Hla drb5 antigen
Immunogenic protection inducing peptide structure
Major histocompatibility antigen class 2
Malaria vaccine
Multiprotein complex
Parasite antibody
Quinine
Recombinant protein
T lymphocyte receptor
Unclassified drug
Hla dr antigen
Lymphocyte antigen receptor
Protein binding
Animal experiment
Animal model
Antibody response
Antibody titer
Antigen binding
Article
Binding affinity
Controlled study
Immunogenetics
Immunological memory
Malaria falciparum
Monkey model
Nonhuman
Parasitemia
Plasmodium falciparum
Priority journal
Provocation test
Animal
Aotus
Binding site
Chemistry
Immunological memory
Immunology
Innate immunity
Malaria
Structure activity relation
Animals
Aotus trivirgatus
Binding sites
Hla-dr beta-chains
Immunologic memory
Malaria
Plasmodium falciparum
Protein binding
Structure-activity relationship
Antimalarial-vaccine
Immunological memory
Mhc-ii
Rotamer-orientation
T-cell-receptor
innate
antigen
t-cell
Immunity
Receptors
Rights
License
Abierto (Texto Completo)
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network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 08b7b42f-4645-4ff5-a2ef-eaccc7f7eab0-18fae7db6-7b9b-4538-b476-6f5ae5a41e7a-14f4671d7-9aa2-44cd-b8f1-b56faf93ba90-179653065-151890881-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-12020-05-26T00:02:42Z2020-05-26T00:02:42Z2016Fully-protective, long-lasting, immunological (FPLLI) memory against Plasmodium falciparum malaria regarding immune protection-inducing protein structures (IMPIPS) vaccinated into monkeys previously challenged and re-challenged 60 days later with a lethal Aotus monkey-adapted P. falciparum strain was found to be associated with preferential high binding capacity to HLA-DR?1* allelic molecules of the major histocompatibility class II (MHC-II), rather than HLA-DR?3*, ?4*, ?5* alleles. Complete PPIIL 3D structure, a longer distance (26.5 Å ± 1.5 Å) between residues perfectly fitting into HLA-DR?1*PBR pockets 1 and 9, a gauche? rotamer orientation in p8 TCR-contacting polar residue and a larger volume of polar p2 residues was also found. This data, in association with previously-described p3 and p7 apolar residues having gauche+ orientation to form a perfect MHC-II-peptide-TCR complex, determines the stereo-electronic and topochemical characteristics associated with FPLLI immunological memory. © 2016 Elsevier Inc.application/pdfhttps://doi.org/10.1016/j.bbrc.2016.06.1150006291X10902104https://repository.urosario.edu.co/handle/10336/23515engElsevier B.V.660No. 4654Biochemical and Biophysical Research CommunicationsVol. 477Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.477, No.4 (2016); pp. 654-660https://www.scopus.com/inward/record.uri?eid=2-s2.0-84979648915&doi=10.1016%2fj.bbrc.2016.06.115&partnerID=40&md5=c174acdba3728a8e15ab2bee01df5a63Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURBinding proteinHla dr antigenHla drb3 antigenHla drb4 antigenHla drb5 antigenImmunogenic protection inducing peptide structureMajor histocompatibility antigen class 2Malaria vaccineMultiprotein complexParasite antibodyQuinineRecombinant proteinT lymphocyte receptorUnclassified drugHla dr antigenLymphocyte antigen receptorProtein bindingAnimal experimentAnimal modelAntibody responseAntibody titerAntigen bindingArticleBinding affinityControlled studyImmunogeneticsImmunological memoryMalaria falciparumMonkey modelNonhumanParasitemiaPlasmodium falciparumPriority journalProvocation testAnimalAotusBinding siteChemistryImmunological memoryImmunologyInnate immunityMalariaStructure activity relationAnimalsAotus trivirgatusBinding sitesHla-dr beta-chainsImmunologic memoryMalariaPlasmodium falciparumProtein bindingStructure-activity relationshipAntimalarial-vaccineImmunological memoryMhc-iiRotamer-orientationT-cell-receptorinnateantigent-cellImmunityReceptorsTCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malariaarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Alba, Martha P.Suarez, Carlos F.Varela, YahsonPatarroyo, Manuel A.Bermudez, AdrianaPatarroyo, Manuel E.10336/23515oai:repository.urosario.edu.co:10336/235152022-05-02 07:37:21.034871https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria
title TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria
spellingShingle TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria
Binding protein
Hla dr antigen
Hla drb3 antigen
Hla drb4 antigen
Hla drb5 antigen
Immunogenic protection inducing peptide structure
Major histocompatibility antigen class 2
Malaria vaccine
Multiprotein complex
Parasite antibody
Quinine
Recombinant protein
T lymphocyte receptor
Unclassified drug
Hla dr antigen
Lymphocyte antigen receptor
Protein binding
Animal experiment
Animal model
Antibody response
Antibody titer
Antigen binding
Article
Binding affinity
Controlled study
Immunogenetics
Immunological memory
Malaria falciparum
Monkey model
Nonhuman
Parasitemia
Plasmodium falciparum
Priority journal
Provocation test
Animal
Aotus
Binding site
Chemistry
Immunological memory
Immunology
Innate immunity
Malaria
Structure activity relation
Animals
Aotus trivirgatus
Binding sites
Hla-dr beta-chains
Immunologic memory
Malaria
Plasmodium falciparum
Protein binding
Structure-activity relationship
Antimalarial-vaccine
Immunological memory
Mhc-ii
Rotamer-orientation
T-cell-receptor
innate
antigen
t-cell
Immunity
Receptors
title_short TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria
title_full TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria
title_fullStr TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria
title_full_unstemmed TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria
title_sort TCR-contacting residues orientation and HLA-DR?* binding preference determine long-lasting protective immunity against malaria
dc.subject.keyword.spa.fl_str_mv Binding protein
Hla dr antigen
Hla drb3 antigen
Hla drb4 antigen
Hla drb5 antigen
Immunogenic protection inducing peptide structure
Major histocompatibility antigen class 2
Malaria vaccine
Multiprotein complex
Parasite antibody
Quinine
Recombinant protein
T lymphocyte receptor
Unclassified drug
Hla dr antigen
Lymphocyte antigen receptor
Protein binding
Animal experiment
Animal model
Antibody response
Antibody titer
Antigen binding
Article
Binding affinity
Controlled study
Immunogenetics
Immunological memory
Malaria falciparum
Monkey model
Nonhuman
Parasitemia
Plasmodium falciparum
Priority journal
Provocation test
Animal
Aotus
Binding site
Chemistry
Immunological memory
Immunology
Innate immunity
Malaria
Structure activity relation
Animals
Aotus trivirgatus
Binding sites
Hla-dr beta-chains
Immunologic memory
Malaria
Plasmodium falciparum
Protein binding
Structure-activity relationship
Antimalarial-vaccine
Immunological memory
Mhc-ii
Rotamer-orientation
T-cell-receptor
topic Binding protein
Hla dr antigen
Hla drb3 antigen
Hla drb4 antigen
Hla drb5 antigen
Immunogenic protection inducing peptide structure
Major histocompatibility antigen class 2
Malaria vaccine
Multiprotein complex
Parasite antibody
Quinine
Recombinant protein
T lymphocyte receptor
Unclassified drug
Hla dr antigen
Lymphocyte antigen receptor
Protein binding
Animal experiment
Animal model
Antibody response
Antibody titer
Antigen binding
Article
Binding affinity
Controlled study
Immunogenetics
Immunological memory
Malaria falciparum
Monkey model
Nonhuman
Parasitemia
Plasmodium falciparum
Priority journal
Provocation test
Animal
Aotus
Binding site
Chemistry
Immunological memory
Immunology
Innate immunity
Malaria
Structure activity relation
Animals
Aotus trivirgatus
Binding sites
Hla-dr beta-chains
Immunologic memory
Malaria
Plasmodium falciparum
Protein binding
Structure-activity relationship
Antimalarial-vaccine
Immunological memory
Mhc-ii
Rotamer-orientation
T-cell-receptor
innate
antigen
t-cell
Immunity
Receptors
dc.subject.keyword.eng.fl_str_mv innate
antigen
t-cell
Immunity
Receptors
description Fully-protective, long-lasting, immunological (FPLLI) memory against Plasmodium falciparum malaria regarding immune protection-inducing protein structures (IMPIPS) vaccinated into monkeys previously challenged and re-challenged 60 days later with a lethal Aotus monkey-adapted P. falciparum strain was found to be associated with preferential high binding capacity to HLA-DR?1* allelic molecules of the major histocompatibility class II (MHC-II), rather than HLA-DR?3*, ?4*, ?5* alleles. Complete PPIIL 3D structure, a longer distance (26.5 Å ± 1.5 Å) between residues perfectly fitting into HLA-DR?1*PBR pockets 1 and 9, a gauche? rotamer orientation in p8 TCR-contacting polar residue and a larger volume of polar p2 residues was also found. This data, in association with previously-described p3 and p7 apolar residues having gauche+ orientation to form a perfect MHC-II-peptide-TCR complex, determines the stereo-electronic and topochemical characteristics associated with FPLLI immunological memory. © 2016 Elsevier Inc.
publishDate 2016
dc.date.created.spa.fl_str_mv 2016
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:42Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:42Z
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.2016.06.115
dc.identifier.issn.none.fl_str_mv 0006291X
10902104
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23515
url https://doi.org/10.1016/j.bbrc.2016.06.115
https://repository.urosario.edu.co/handle/10336/23515
identifier_str_mv 0006291X
10902104
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 660
dc.relation.citationIssue.none.fl_str_mv No. 4
dc.relation.citationStartPage.none.fl_str_mv 654
dc.relation.citationTitle.none.fl_str_mv Biochemical and Biophysical Research Communications
dc.relation.citationVolume.none.fl_str_mv Vol. 477
dc.relation.ispartof.spa.fl_str_mv Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.477, No.4 (2016); pp. 654-660
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-84979648915&doi=10.1016%2fj.bbrc.2016.06.115&partnerID=40&md5=c174acdba3728a8e15ab2bee01df5a63
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
dc.publisher.spa.fl_str_mv Elsevier B.V.
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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