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...
- 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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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 |
_version_ |
1814167496349974528 |