Malaria parasite survival depends on conserved binding peptides’ critical biological functions

Biochemical, structural and single amino acid level analysis of 49 Plasmodium falciparum protein regions (13 sporozoite and 36 merozoite proteins) has highlighted the functional role of each conserved high activity binding peptide (cHABP) in cell host-microbe interaction, involving biological functi...

Full description

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:10336/23812
Acceso en línea:
https://repository.urosario.edu.co/handle/10336/23812
Palabra clave:
Calcium ion
Conserved high activity binding peptide
Epidermal growth factor
Erythrocyte membrane protein 1
Membrane protein
Microorganism protein
Protein clag 3 2
Protein csp 1
Protein msp1
Protein msp2
Protein pf12
Protein pf38
Protein pf41
Protein pfrh
Protein ptramp
Protein rama
Protein rh2a
Protein rh2b
Protein rh4
Protein rhoph3
Sialic acid
Unclassified drug
Peptide
Protozoal protein
Amino acid sequence
Article
Binding site
Disease association
Erythrocyte
Host parasite interaction
Human
Liver
Malaria
Merozoite
Nonhuman
Parasite migration
Parasite survival
Plasmodium falciparum
Protein binding
Protein domain
Protein expression
Regulatory mechanism
Sporozoite
Tight junction
Hep-g2 cell line
Host parasite interaction
Malaria falciparum
Parasitology
Physiology
Plasmodium falciparum
Erythrocytes
Hep g2 cells
Host-parasite interactions
Humans
Peptides
Plasmodium falciparum
Protozoan proteins
Sporozoites
falciparum
Malaria
Rights
License
Abierto (Texto Completo)
id EDOCUR2_5d42bae1e98fa6f02bb7b225ed7a3cfb
oai_identifier_str oai:repository.urosario.edu.co:10336/23812
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 76e03223-040d-4e46-864f-3bdecc8d2790-172114b23-9a0b-4914-a288-3ac7305d4eed-1a4805c8d-6c48-42be-9936-39c146a5f350-1e77c244a-2cd7-4aca-bd38-0a2a5524f917-19fc64f6d-a903-48f1-ac2e-4e55fd2ed9af-12020-05-26T00:05:38Z2020-05-26T00:05:38Z2016Biochemical, structural and single amino acid level analysis of 49 Plasmodium falciparum protein regions (13 sporozoite and 36 merozoite proteins) has highlighted the functional role of each conserved high activity binding peptide (cHABP) in cell host-microbe interaction, involving biological functions such as gliding motility, traversal activity, binding invasion, reproduction, nutrient ion transport and the development of severe malaria. Each protein's key function in the malaria parasite's asexual lifecycle (pre-erythrocyte and erythro-cyte) is described in terms of cHABPs; their sequences were located in elegant work published by other groups regarding critical binding regions implicated in malarial parasite invasion. Such cHABPs represent the starting point for developing a logical and rational methodology for selecting an appropriate mixture of modified cHABPs to be used in a completely effective, synthetic antimalarial vaccine. Such methodology could be used for developing vaccines against diseases scourging humanity. © 2016, Caister Academic Press. All rights reserved.application/pdf1467303714673045https://repository.urosario.edu.co/handle/10336/23812engCaister Academic Press78No. 157Current Issues in Molecular BiologyVol. 18Current Issues in Molecular Biology, ISSN:14673037, 14673045, Vol.18, No.1 (2016); pp. 57-78https://www.scopus.com/inward/record.uri?eid=2-s2.0-84941005868&partnerID=40&md5=5ffb310e3d89a6d468a8a12959b1799bAbierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURCalcium ionConserved high activity binding peptideEpidermal growth factorErythrocyte membrane protein 1Membrane proteinMicroorganism proteinProtein clag 3 2Protein csp 1Protein msp1Protein msp2Protein pf12Protein pf38Protein pf41Protein pfrhProtein ptrampProtein ramaProtein rh2aProtein rh2bProtein rh4Protein rhoph3Sialic acidUnclassified drugPeptideProtozoal proteinAmino acid sequenceArticleBinding siteDisease associationErythrocyteHost parasite interactionHumanLiverMalariaMerozoiteNonhumanParasite migrationParasite survivalPlasmodium falciparumProtein bindingProtein domainProtein expressionRegulatory mechanismSporozoiteTight junctionHep-g2 cell lineHost parasite interactionMalaria falciparumParasitologyPhysiologyPlasmodium falciparumErythrocytesHep g2 cellsHost-parasite interactionsHumansPeptidesPlasmodium falciparumProtozoan proteinsSporozoitesfalciparumMalariaMalaria parasite survival depends on conserved binding peptides’ critical biological functionsarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Patarroyo M.E.Arévalo-Pinzón G.Reyes C.Moreno-Vranich A.Patarroyo M.A.10336/23812oai:repository.urosario.edu.co:10336/238122022-05-02 07:37:14.813376https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Malaria parasite survival depends on conserved binding peptides’ critical biological functions
title Malaria parasite survival depends on conserved binding peptides’ critical biological functions
spellingShingle Malaria parasite survival depends on conserved binding peptides’ critical biological functions
Calcium ion
Conserved high activity binding peptide
Epidermal growth factor
Erythrocyte membrane protein 1
Membrane protein
Microorganism protein
Protein clag 3 2
Protein csp 1
Protein msp1
Protein msp2
Protein pf12
Protein pf38
Protein pf41
Protein pfrh
Protein ptramp
Protein rama
Protein rh2a
Protein rh2b
Protein rh4
Protein rhoph3
Sialic acid
Unclassified drug
Peptide
Protozoal protein
Amino acid sequence
Article
Binding site
Disease association
Erythrocyte
Host parasite interaction
Human
Liver
Malaria
Merozoite
Nonhuman
Parasite migration
Parasite survival
Plasmodium falciparum
Protein binding
Protein domain
Protein expression
Regulatory mechanism
Sporozoite
Tight junction
Hep-g2 cell line
Host parasite interaction
Malaria falciparum
Parasitology
Physiology
Plasmodium falciparum
Erythrocytes
Hep g2 cells
Host-parasite interactions
Humans
Peptides
Plasmodium falciparum
Protozoan proteins
Sporozoites
falciparum
Malaria
title_short Malaria parasite survival depends on conserved binding peptides’ critical biological functions
title_full Malaria parasite survival depends on conserved binding peptides’ critical biological functions
title_fullStr Malaria parasite survival depends on conserved binding peptides’ critical biological functions
title_full_unstemmed Malaria parasite survival depends on conserved binding peptides’ critical biological functions
title_sort Malaria parasite survival depends on conserved binding peptides’ critical biological functions
dc.subject.keyword.spa.fl_str_mv Calcium ion
Conserved high activity binding peptide
Epidermal growth factor
Erythrocyte membrane protein 1
Membrane protein
Microorganism protein
Protein clag 3 2
Protein csp 1
Protein msp1
Protein msp2
Protein pf12
Protein pf38
Protein pf41
Protein pfrh
Protein ptramp
Protein rama
Protein rh2a
Protein rh2b
Protein rh4
Protein rhoph3
Sialic acid
Unclassified drug
Peptide
Protozoal protein
Amino acid sequence
Article
Binding site
Disease association
Erythrocyte
Host parasite interaction
Human
Liver
Malaria
Merozoite
Nonhuman
Parasite migration
Parasite survival
Plasmodium falciparum
Protein binding
Protein domain
Protein expression
Regulatory mechanism
Sporozoite
Tight junction
Hep-g2 cell line
Host parasite interaction
Malaria falciparum
Parasitology
Physiology
Plasmodium falciparum
Erythrocytes
Hep g2 cells
Host-parasite interactions
Humans
Peptides
Plasmodium falciparum
Protozoan proteins
Sporozoites
topic Calcium ion
Conserved high activity binding peptide
Epidermal growth factor
Erythrocyte membrane protein 1
Membrane protein
Microorganism protein
Protein clag 3 2
Protein csp 1
Protein msp1
Protein msp2
Protein pf12
Protein pf38
Protein pf41
Protein pfrh
Protein ptramp
Protein rama
Protein rh2a
Protein rh2b
Protein rh4
Protein rhoph3
Sialic acid
Unclassified drug
Peptide
Protozoal protein
Amino acid sequence
Article
Binding site
Disease association
Erythrocyte
Host parasite interaction
Human
Liver
Malaria
Merozoite
Nonhuman
Parasite migration
Parasite survival
Plasmodium falciparum
Protein binding
Protein domain
Protein expression
Regulatory mechanism
Sporozoite
Tight junction
Hep-g2 cell line
Host parasite interaction
Malaria falciparum
Parasitology
Physiology
Plasmodium falciparum
Erythrocytes
Hep g2 cells
Host-parasite interactions
Humans
Peptides
Plasmodium falciparum
Protozoan proteins
Sporozoites
falciparum
Malaria
dc.subject.keyword.eng.fl_str_mv falciparum
Malaria
description Biochemical, structural and single amino acid level analysis of 49 Plasmodium falciparum protein regions (13 sporozoite and 36 merozoite proteins) has highlighted the functional role of each conserved high activity binding peptide (cHABP) in cell host-microbe interaction, involving biological functions such as gliding motility, traversal activity, binding invasion, reproduction, nutrient ion transport and the development of severe malaria. Each protein's key function in the malaria parasite's asexual lifecycle (pre-erythrocyte and erythro-cyte) is described in terms of cHABPs; their sequences were located in elegant work published by other groups regarding critical binding regions implicated in malarial parasite invasion. Such cHABPs represent the starting point for developing a logical and rational methodology for selecting an appropriate mixture of modified cHABPs to be used in a completely effective, synthetic antimalarial vaccine. Such methodology could be used for developing vaccines against diseases scourging humanity. © 2016, Caister Academic Press. All rights reserved.
publishDate 2016
dc.date.created.spa.fl_str_mv 2016
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:05:38Z
dc.date.available.none.fl_str_mv 2020-05-26T00:05:38Z
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.issn.none.fl_str_mv 14673037
14673045
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23812
identifier_str_mv 14673037
14673045
url https://repository.urosario.edu.co/handle/10336/23812
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 78
dc.relation.citationIssue.none.fl_str_mv No. 1
dc.relation.citationStartPage.none.fl_str_mv 57
dc.relation.citationTitle.none.fl_str_mv Current Issues in Molecular Biology
dc.relation.citationVolume.none.fl_str_mv Vol. 18
dc.relation.ispartof.spa.fl_str_mv Current Issues in Molecular Biology, ISSN:14673037, 14673045, Vol.18, No.1 (2016); pp. 57-78
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-84941005868&partnerID=40&md5=5ffb310e3d89a6d468a8a12959b1799b
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 Caister Academic Press
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_ 1814167605537144832

Publicaciones similares