TCR-contacting residues orientation and HLA-DRβ* binding preference determine long-lasting protective immunity against malaria

Martha P. Alba, Carlos F. Suarez, Yahson Varela, Manuel A. Patarroyo, Adriana Bermudez, Manuel E. Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

4 Citas (Scopus)

Resumen

© 2016 Elsevier Inc.Fully-protective, long-lasting, immunological (FPLLI) memory against Plasmodium falciparum malaria regarding immune protection-inducing protein structures (IMPIPS) vaccinated into monkeys previously challenged and re-challenged 60 days later with a lethal Aotus monkey-adapted P. falciparum strain was found to be associated with preferential high binding capacity to HLA-DRβ1* allelic molecules of the major histocompatibility class II (MHC-II), rather than HLA-DRβ3*, β4*, β5* alleles. Complete PPIIL 3D structure, a longer distance (26.5 Å ± 1.5 Å) between residues perfectly fitting into HLA-DRβ1*PBR pockets 1 and 9, a gauche− rotamer orientation in p8 TCR-contacting polar residue and a larger volume of polar p2 residues was also found. This data, in association with previously-described p3 and p7 apolar residues having gauche+ orientation to form a perfect MHC-II-peptide-TCR complex, determines the stereo-electronic and topochemical characteristics associated with FPLLI immunological memory.
Idioma originalEnglish (US)
Páginas (desde-hasta)654-660
Número de páginas7
PublicaciónBiochemical and Biophysical Research Communications
DOI
EstadoPublished - sep 2 2016

Huella dactilar

Immunologic Memory
Histocompatibility
Malaria
Haplorhini
Immunity
Data storage equipment
Falciparum Malaria
Plasmodium falciparum
Alleles
Peptides
Molecules
Proteins

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title = "TCR-contacting residues orientation and HLA-DRβ* binding preference determine long-lasting protective immunity against malaria",
abstract = "{\circledC} 2016 Elsevier Inc.Fully-protective, long-lasting, immunological (FPLLI) memory against Plasmodium falciparum malaria regarding immune protection-inducing protein structures (IMPIPS) vaccinated into monkeys previously challenged and re-challenged 60 days later with a lethal Aotus monkey-adapted P. falciparum strain was found to be associated with preferential high binding capacity to HLA-DRβ1* allelic molecules of the major histocompatibility class II (MHC-II), rather than HLA-DRβ3*, β4*, β5* alleles. Complete PPIIL 3D structure, a longer distance (26.5 {\AA} ± 1.5 {\AA}) between residues perfectly fitting into HLA-DRβ1*PBR pockets 1 and 9, a gauche− rotamer orientation in p8 TCR-contacting polar residue and a larger volume of polar p2 residues was also found. This data, in association with previously-described p3 and p7 apolar residues having gauche+ orientation to form a perfect MHC-II-peptide-TCR complex, determines the stereo-electronic and topochemical characteristics associated with FPLLI immunological memory.",
author = "Alba, {Martha P.} and Suarez, {Carlos F.} and Yahson Varela and Patarroyo, {Manuel A.} and Adriana Bermudez and Patarroyo, {Manuel E.}",
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TCR-contacting residues orientation and HLA-DRβ* binding preference determine long-lasting protective immunity against malaria. / Alba, Martha P.; Suarez, Carlos F.; Varela, Yahson; Patarroyo, Manuel A.; Bermudez, Adriana; Patarroyo, Manuel E.

En: Biochemical and Biophysical Research Communications, 02.09.2016, p. 654-660.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - TCR-contacting residues orientation and HLA-DRβ* binding preference determine long-lasting protective immunity against malaria

AU - Alba, Martha P.

AU - Suarez, Carlos F.

AU - Varela, Yahson

AU - Patarroyo, Manuel A.

AU - Bermudez, Adriana

AU - Patarroyo, Manuel E.

PY - 2016/9/2

Y1 - 2016/9/2

N2 - © 2016 Elsevier Inc.Fully-protective, long-lasting, immunological (FPLLI) memory against Plasmodium falciparum malaria regarding immune protection-inducing protein structures (IMPIPS) vaccinated into monkeys previously challenged and re-challenged 60 days later with a lethal Aotus monkey-adapted P. falciparum strain was found to be associated with preferential high binding capacity to HLA-DRβ1* allelic molecules of the major histocompatibility class II (MHC-II), rather than HLA-DRβ3*, β4*, β5* alleles. Complete PPIIL 3D structure, a longer distance (26.5 Å ± 1.5 Å) between residues perfectly fitting into HLA-DRβ1*PBR pockets 1 and 9, a gauche− rotamer orientation in p8 TCR-contacting polar residue and a larger volume of polar p2 residues was also found. This data, in association with previously-described p3 and p7 apolar residues having gauche+ orientation to form a perfect MHC-II-peptide-TCR complex, determines the stereo-electronic and topochemical characteristics associated with FPLLI immunological memory.

AB - © 2016 Elsevier Inc.Fully-protective, long-lasting, immunological (FPLLI) memory against Plasmodium falciparum malaria regarding immune protection-inducing protein structures (IMPIPS) vaccinated into monkeys previously challenged and re-challenged 60 days later with a lethal Aotus monkey-adapted P. falciparum strain was found to be associated with preferential high binding capacity to HLA-DRβ1* allelic molecules of the major histocompatibility class II (MHC-II), rather than HLA-DRβ3*, β4*, β5* alleles. Complete PPIIL 3D structure, a longer distance (26.5 Å ± 1.5 Å) between residues perfectly fitting into HLA-DRβ1*PBR pockets 1 and 9, a gauche− rotamer orientation in p8 TCR-contacting polar residue and a larger volume of polar p2 residues was also found. This data, in association with previously-described p3 and p7 apolar residues having gauche+ orientation to form a perfect MHC-II-peptide-TCR complex, determines the stereo-electronic and topochemical characteristics associated with FPLLI immunological memory.

U2 - 10.1016/j.bbrc.2016.06.115

DO - 10.1016/j.bbrc.2016.06.115

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JF - Biochemical and Biophysical Research Communications

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