Vista Equipo: The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles

The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles

The importance of CSP- and STARP-derived ? and ? dihedral angles in mHABP structure was analysed by 1H NMR in the search for molecules which can be included as components of a first-line-of-defence Plasmodium falciparum sporozoite multi-epitope vaccine against the most lethal form of human malaria....

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Autores Principales:	Patarroyo, Manuel E., Bermudez, Adriana, Alba, Martha P.
Formato:	Artículo (Article)
Lenguaje:	Inglés (English)
Publicado:	2012
Materias:	Binding protein Circumsporozoite protein High activity binding peptide Major histocompatibility antigen class 2 Proline Protozoal protein Sporozoite threonine and asparagine rich protein Sporozoite vaccine Unclassified drug Alpha helix Amino acid sequence Article Complex formation Hydrogen bond Immunogenicity Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Animals Aotus trivirgatus Hla-dr beta-chains Humans Malaria vaccines Molecular sequence data Peptide fragments Peptides Protozoan proteins Sporozoites ? and ? angles Antimalarial-vaccine Hladr?* molecules Pre-erythrocyte stage secondary protozoan biomolecular Antigens Nuclear magnetic resonance
Acceso en línea:	https://repository.urosario.edu.co/handle/10336/23512 https://doi.org/10.1016/j.bbrc.2012.10.088

id	ir-10336-23512
recordtype	dspace
spelling	ir-10336-235122022-05-02T12:37:21Z The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles Patarroyo, Manuel E. Bermudez, Adriana Alba, Martha P. Binding protein Circumsporozoite protein High activity binding peptide Major histocompatibility antigen class 2 Proline Protozoal protein Sporozoite threonine and asparagine rich protein Sporozoite vaccine Unclassified drug Alpha helix Amino acid sequence Article Complex formation Hydrogen bond Immunogenicity Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Amino acid sequence Animals Aotus trivirgatus Hla-dr beta-chains Humans Malaria vaccines Molecular sequence data Peptide fragments Peptides Plasmodium falciparum Protozoan proteins Sporozoites Plasmodium falciparum ? and ? angles Antimalarial-vaccine Hladr?* molecules Plasmodium falciparum Pre-erythrocyte stage secondary protozoan biomolecular Antigens Nuclear magnetic resonance Protein structure The importance of CSP- and STARP-derived ? and ? dihedral angles in mHABP structure was analysed by 1H NMR in the search for molecules which can be included as components of a first-line-of-defence Plasmodium falciparum sporozoite multi-epitope vaccine against the most lethal form of human malaria. Most of the aforementioned dihedral angles were left-hand-like polyproline type II (PPIIL) structures whilst others had right-hand-like ?-helix (?R), thus allowing mHABPS to fit better into MHCII molecules and thereby form an appropriate pMHCII complex and also establish the H-bonds which stabilise such complex and by this means induce an appropriate immune response. This information has great implications for vaccine development, malaria being one of them. © 2012 Elsevier Inc. 2012 2020-05-26T00:02:39Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 0006291X 10902104 https://repository.urosario.edu.co/handle/10336/23512 https://doi.org/10.1016/j.bbrc.2012.10.088 eng info:eu-repo/semantics/openAccess application/pdf instname:Universidad del Rosario
institution	EdocUR - Universidad del Rosario
collection	DSpace
language	Inglés (English)
topic	Binding protein Circumsporozoite protein High activity binding peptide Major histocompatibility antigen class 2 Proline Protozoal protein Sporozoite threonine and asparagine rich protein Sporozoite vaccine Unclassified drug Alpha helix Amino acid sequence Article Complex formation Hydrogen bond Immunogenicity Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Amino acid sequence Animals Aotus trivirgatus Hla-dr beta-chains Humans Malaria vaccines Molecular sequence data Peptide fragments Peptides Plasmodium falciparum Protozoan proteins Sporozoites Plasmodium falciparum ? and ? angles Antimalarial-vaccine Hladr?* molecules Plasmodium falciparum Pre-erythrocyte stage secondary protozoan biomolecular Antigens Nuclear magnetic resonance Protein structure
spellingShingle	Binding protein Circumsporozoite protein High activity binding peptide Major histocompatibility antigen class 2 Proline Protozoal protein Sporozoite threonine and asparagine rich protein Sporozoite vaccine Unclassified drug Alpha helix Amino acid sequence Article Complex formation Hydrogen bond Immunogenicity Plasmodium falciparum Priority journal Protein structure Proton nuclear magnetic resonance Amino acid sequence Animals Aotus trivirgatus Hla-dr beta-chains Humans Malaria vaccines Molecular sequence data Peptide fragments Peptides Plasmodium falciparum Protozoan proteins Sporozoites Plasmodium falciparum ? and ? angles Antimalarial-vaccine Hladr?* molecules Plasmodium falciparum Pre-erythrocyte stage secondary protozoan biomolecular Antigens Nuclear magnetic resonance Protein structure Patarroyo, Manuel E. Bermudez, Adriana Alba, Martha P. The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
description	The importance of CSP- and STARP-derived ? and ? dihedral angles in mHABP structure was analysed by 1H NMR in the search for molecules which can be included as components of a first-line-of-defence Plasmodium falciparum sporozoite multi-epitope vaccine against the most lethal form of human malaria. Most of the aforementioned dihedral angles were left-hand-like polyproline type II (PPIIL) structures whilst others had right-hand-like ?-helix (?R), thus allowing mHABPS to fit better into MHCII molecules and thereby form an appropriate pMHCII complex and also establish the H-bonds which stabilise such complex and by this means induce an appropriate immune response. This information has great implications for vaccine development, malaria being one of them. © 2012 Elsevier Inc.
format	Artículo (Article)
author	Patarroyo, Manuel E. Bermudez, Adriana Alba, Martha P.
author_facet	Patarroyo, Manuel E. Bermudez, Adriana Alba, Martha P.
author_sort	Patarroyo, Manuel E.
title	The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
title_short	The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
title_full	The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
title_fullStr	The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
title_full_unstemmed	The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
title_sort	high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles
publishDate	2012
url	https://repository.urosario.edu.co/handle/10336/23512 https://doi.org/10.1016/j.bbrc.2012.10.088
_version_	1740172234290364416
score	12,131701

The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles

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