Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria

Based on the 3D X-ray crystallographic structures of relevant proteins of the malaria parasite involved in invasion to host cells and 3D NMR structures of High Activity Binding Peptides (HABPs) and their respective analogues, it was found that HABPs are rendered into highly immunogenic and sterile i...

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Autores:
Tipo de recurso:
Fecha de publicación:
2010
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23507
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2010.03.004
https://repository.urosario.edu.co/handle/10336/23507
Palabra clave:
Malaria vaccine
Parasite antigen
Amino acid composition
Animal experiment
Animal model
Aotus
Article
Controlled study
Host resistance
Hydrogen bond
Immunogenicity
Malaria falciparum
Nonhuman
Physical chemistry
Plasmodium falciparum
Priority journal
Vaccine production
Amino acid sequence
Animals
Aotus trivirgatus
Host-parasite interactions
Hydrogen bonding
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Protein conformation
Plasmodium falciparum
H-bonds
Malaria
Plasmodium falciparum
Sterile immunity
x-ray
protozoan
protozoan
biomolecular
Antibodies
Antigens
Crystallography
Nuclear magnetic resonance
Rights
License
Abierto (Texto Completo)
id EDOCUR2_5153387c5a8e7dcc750d3c0608fcc368
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network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
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spelling 10ecd4f9-843f-4ef2-bec0-7d39d3381a13-1d39495d0-c601-4370-a993-42b78fd63e7d-13be70745-3969-4b41-af6a-d31f4ae51031-101a1c86e-e857-46fd-8fa7-3664f825e9ba-1517210186002020-05-26T00:02:37Z2020-05-26T00:02:37Z2010Based on the 3D X-ray crystallographic structures of relevant proteins of the malaria parasite involved in invasion to host cells and 3D NMR structures of High Activity Binding Peptides (HABPs) and their respective analogues, it was found that HABPs are rendered into highly immunogenic and sterile immunity inducers in the Aotus experimental model by modifying those amino acids that establish H-bonds with other HABPs or binding to host's cells. This finding adds striking and novel physicochemical principles, at the atomic level, for a logical and rational vaccine development methodology against infectious disease, among them malaria. © 2010 Elsevier Inc. All rights reserved.application/pdfhttps://doi.org/10.1016/j.bbrc.2010.03.0040006291X10902104https://repository.urosario.edu.co/handle/10336/23507eng535No. 3529Biochemical and Biophysical Research CommunicationsVol. 394Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.394, No.3 (2010); pp. 529-535https://www.scopus.com/inward/record.uri?eid=2-s2.0-77950517324&doi=10.1016%2fj.bbrc.2010.03.004&partnerID=40&md5=81f947136ff0a7d59323b1ed3dcd4001Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURMalaria vaccineParasite antigenAmino acid compositionAnimal experimentAnimal modelAotusArticleControlled studyHost resistanceHydrogen bondImmunogenicityMalaria falciparumNonhumanPhysical chemistryPlasmodium falciparumPriority journalVaccine productionAmino acid sequenceAnimalsAotus trivirgatusHost-parasite interactionsHydrogen bondingMalariaMalaria vaccinesMolecular sequence dataPeptidesProtein conformationPlasmodium falciparumH-bondsMalariaPlasmodium falciparumSterile immunityx-rayprotozoanprotozoanbiomolecularAntibodiesAntigensCrystallographyNuclear magnetic resonanceAtomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malariaarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Patarroyo, Manuel E.Cifuentes, GladysPiraján, CamiloMoreno-Vranich, ArmandoVanegas, Magnolia10336/23507oai:repository.urosario.edu.co:10336/235072022-05-02 07:37:21.028923https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
title Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
spellingShingle Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
Malaria vaccine
Parasite antigen
Amino acid composition
Animal experiment
Animal model
Aotus
Article
Controlled study
Host resistance
Hydrogen bond
Immunogenicity
Malaria falciparum
Nonhuman
Physical chemistry
Plasmodium falciparum
Priority journal
Vaccine production
Amino acid sequence
Animals
Aotus trivirgatus
Host-parasite interactions
Hydrogen bonding
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Protein conformation
Plasmodium falciparum
H-bonds
Malaria
Plasmodium falciparum
Sterile immunity
x-ray
protozoan
protozoan
biomolecular
Antibodies
Antigens
Crystallography
Nuclear magnetic resonance
title_short Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
title_full Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
title_fullStr Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
title_full_unstemmed Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
title_sort Atomic evidence that modification of H-bonds established with amino acids critical for host-cell binding induces sterile immunity against malaria
dc.subject.keyword.spa.fl_str_mv Malaria vaccine
Parasite antigen
Amino acid composition
Animal experiment
Animal model
Aotus
Article
Controlled study
Host resistance
Hydrogen bond
Immunogenicity
Malaria falciparum
Nonhuman
Physical chemistry
Plasmodium falciparum
Priority journal
Vaccine production
Amino acid sequence
Animals
Aotus trivirgatus
Host-parasite interactions
Hydrogen bonding
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Protein conformation
Plasmodium falciparum
H-bonds
Malaria
Plasmodium falciparum
Sterile immunity
topic Malaria vaccine
Parasite antigen
Amino acid composition
Animal experiment
Animal model
Aotus
Article
Controlled study
Host resistance
Hydrogen bond
Immunogenicity
Malaria falciparum
Nonhuman
Physical chemistry
Plasmodium falciparum
Priority journal
Vaccine production
Amino acid sequence
Animals
Aotus trivirgatus
Host-parasite interactions
Hydrogen bonding
Malaria
Malaria vaccines
Molecular sequence data
Peptides
Protein conformation
Plasmodium falciparum
H-bonds
Malaria
Plasmodium falciparum
Sterile immunity
x-ray
protozoan
protozoan
biomolecular
Antibodies
Antigens
Crystallography
Nuclear magnetic resonance
dc.subject.keyword.eng.fl_str_mv x-ray
protozoan
protozoan
biomolecular
Antibodies
Antigens
Crystallography
Nuclear magnetic resonance
description Based on the 3D X-ray crystallographic structures of relevant proteins of the malaria parasite involved in invasion to host cells and 3D NMR structures of High Activity Binding Peptides (HABPs) and their respective analogues, it was found that HABPs are rendered into highly immunogenic and sterile immunity inducers in the Aotus experimental model by modifying those amino acids that establish H-bonds with other HABPs or binding to host's cells. This finding adds striking and novel physicochemical principles, at the atomic level, for a logical and rational vaccine development methodology against infectious disease, among them malaria. © 2010 Elsevier Inc. All rights reserved.
publishDate 2010
dc.date.created.spa.fl_str_mv 2010
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:02:37Z
dc.date.available.none.fl_str_mv 2020-05-26T00:02:37Z
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.2010.03.004
dc.identifier.issn.none.fl_str_mv 0006291X
10902104
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23507
url https://doi.org/10.1016/j.bbrc.2010.03.004
https://repository.urosario.edu.co/handle/10336/23507
identifier_str_mv 0006291X
10902104
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 535
dc.relation.citationIssue.none.fl_str_mv No. 3
dc.relation.citationStartPage.none.fl_str_mv 529
dc.relation.citationTitle.none.fl_str_mv Biochemical and Biophysical Research Communications
dc.relation.citationVolume.none.fl_str_mv Vol. 394
dc.relation.ispartof.spa.fl_str_mv Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.394, No.3 (2010); pp. 529-535
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-77950517324&doi=10.1016%2fj.bbrc.2010.03.004&partnerID=40&md5=81f947136ff0a7d59323b1ed3dcd4001
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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