Atomic fidelity of subunit-based chemically-synthesized antimalarial vaccine components

Manuel E. Patarroyo, Gladys Cifuentes, Nora L. Martínez, Manuel A. Patarroyo

Research output: Contribution to journalLiterature review

14 Citations (Scopus)

Abstract

The tri-dimensional (3D) structure determined by NMR of functionally relevant High Activity Binding Peptides (HABPs) of chemically-synthesized malarial proteins, involved in invasion to target cells, is practically identical, at the atomic level, to their corresponding recombinantly produced proteins, determined by X-ray crystallography. Both recombinant proteins as well as these chemically-synthesized HABPs bind to host-cell receptors through channels or troughs formation, stabilized by hydrogen bonding; most of them are located on distant segments to the highly polymorphic, highly antigenic, strain specific amino acid sequences the parasite uses to evade immune pressure. When these immunologically silent conserved HABPs are specifically modified, they become highly immunogenic and capable of inducing protective immune responses, supporting the specifically modified minimal subunit-based, multiepitopic, chemically-synthesized vaccines concept. © 2009 Elsevier Ltd. All rights reserved.
Original languageEnglish (US)
Pages (from-to)38-44
Number of pages7
JournalProgress in Biophysics and Molecular Biology
DOIs
StatePublished - Jan 1 2010

Fingerprint

Antimalarials
Vaccines
Peptides
X Ray Crystallography
Hydrogen Bonding
Recombinant Proteins
Amino Acid Sequence
Parasites
Proteins
Pressure

Cite this

@article{8c76dffa3fc74c8186d85bff762512d7,
title = "Atomic fidelity of subunit-based chemically-synthesized antimalarial vaccine components",
abstract = "The tri-dimensional (3D) structure determined by NMR of functionally relevant High Activity Binding Peptides (HABPs) of chemically-synthesized malarial proteins, involved in invasion to target cells, is practically identical, at the atomic level, to their corresponding recombinantly produced proteins, determined by X-ray crystallography. Both recombinant proteins as well as these chemically-synthesized HABPs bind to host-cell receptors through channels or troughs formation, stabilized by hydrogen bonding; most of them are located on distant segments to the highly polymorphic, highly antigenic, strain specific amino acid sequences the parasite uses to evade immune pressure. When these immunologically silent conserved HABPs are specifically modified, they become highly immunogenic and capable of inducing protective immune responses, supporting the specifically modified minimal subunit-based, multiepitopic, chemically-synthesized vaccines concept. {\circledC} 2009 Elsevier Ltd. All rights reserved.",
author = "Patarroyo, {Manuel E.} and Gladys Cifuentes and Mart{\'i}nez, {Nora L.} and Patarroyo, {Manuel A.}",
year = "2010",
month = "1",
day = "1",
doi = "10.1016/j.pbiomolbio.2009.10.006",
language = "English (US)",
pages = "38--44",
journal = "Progress in Biophysics and Molecular Biology",
issn = "0079-6107",
publisher = "Elsevier Limited",

}

Atomic fidelity of subunit-based chemically-synthesized antimalarial vaccine components. / Patarroyo, Manuel E.; Cifuentes, Gladys; Martínez, Nora L.; Patarroyo, Manuel A.

In: Progress in Biophysics and Molecular Biology, 01.01.2010, p. 38-44.

Research output: Contribution to journalLiterature review

TY - JOUR

T1 - Atomic fidelity of subunit-based chemically-synthesized antimalarial vaccine components

AU - Patarroyo, Manuel E.

AU - Cifuentes, Gladys

AU - Martínez, Nora L.

AU - Patarroyo, Manuel A.

PY - 2010/1/1

Y1 - 2010/1/1

N2 - The tri-dimensional (3D) structure determined by NMR of functionally relevant High Activity Binding Peptides (HABPs) of chemically-synthesized malarial proteins, involved in invasion to target cells, is practically identical, at the atomic level, to their corresponding recombinantly produced proteins, determined by X-ray crystallography. Both recombinant proteins as well as these chemically-synthesized HABPs bind to host-cell receptors through channels or troughs formation, stabilized by hydrogen bonding; most of them are located on distant segments to the highly polymorphic, highly antigenic, strain specific amino acid sequences the parasite uses to evade immune pressure. When these immunologically silent conserved HABPs are specifically modified, they become highly immunogenic and capable of inducing protective immune responses, supporting the specifically modified minimal subunit-based, multiepitopic, chemically-synthesized vaccines concept. © 2009 Elsevier Ltd. All rights reserved.

AB - The tri-dimensional (3D) structure determined by NMR of functionally relevant High Activity Binding Peptides (HABPs) of chemically-synthesized malarial proteins, involved in invasion to target cells, is practically identical, at the atomic level, to their corresponding recombinantly produced proteins, determined by X-ray crystallography. Both recombinant proteins as well as these chemically-synthesized HABPs bind to host-cell receptors through channels or troughs formation, stabilized by hydrogen bonding; most of them are located on distant segments to the highly polymorphic, highly antigenic, strain specific amino acid sequences the parasite uses to evade immune pressure. When these immunologically silent conserved HABPs are specifically modified, they become highly immunogenic and capable of inducing protective immune responses, supporting the specifically modified minimal subunit-based, multiepitopic, chemically-synthesized vaccines concept. © 2009 Elsevier Ltd. All rights reserved.

U2 - 10.1016/j.pbiomolbio.2009.10.006

DO - 10.1016/j.pbiomolbio.2009.10.006

M3 - Literature review

C2 - 19961869

SP - 38

EP - 44

JO - Progress in Biophysics and Molecular Biology

JF - Progress in Biophysics and Molecular Biology

SN - 0079-6107

ER -