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...
- 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 |
---|---|
oai_identifier_str |
oai:repository.urosario.edu.co:10336/23507 |
network_acronym_str |
EDOCUR2 |
network_name_str |
Repositorio EdocUR - U. Rosario |
repository_id_str |
|
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 |
_version_ |
1814167510216343552 |