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

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 wa...

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:10336/23515
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2016.06.115
https://repository.urosario.edu.co/handle/10336/23515
Palabra clave:
Binding protein
Hla dr antigen
Hla drb3 antigen
Hla drb4 antigen
Hla drb5 antigen
Immunogenic protection inducing peptide structure
Major histocompatibility antigen class 2
Malaria vaccine
Multiprotein complex
Parasite antibody
Quinine
Recombinant protein
T lymphocyte receptor
Unclassified drug
Hla dr antigen
Lymphocyte antigen receptor
Protein binding
Animal experiment
Animal model
Antibody response
Antibody titer
Antigen binding
Article
Binding affinity
Controlled study
Immunogenetics
Immunological memory
Malaria falciparum
Monkey model
Nonhuman
Parasitemia
Plasmodium falciparum
Priority journal
Provocation test
Animal
Aotus
Binding site
Chemistry
Immunological memory
Immunology
Innate immunity
Malaria
Structure activity relation
Animals
Aotus trivirgatus
Binding sites
Hla-dr beta-chains
Immunologic memory
Malaria
Plasmodium falciparum
Protein binding
Structure-activity relationship
Antimalarial-vaccine
Immunological memory
Mhc-ii
Rotamer-orientation
T-cell-receptor
innate
antigen
t-cell
Immunity
Receptors
Rights
License
Abierto (Texto Completo)
Description
Summary: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-DR?1* allelic molecules of the major histocompatibility class II (MHC-II), rather than HLA-DR?3*, ?4*, ?5* alleles. Complete PPIIL 3D structure, a longer distance (26.5 Å ± 1.5 Å) between residues perfectly fitting into HLA-DR?1*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. © 2016 Elsevier Inc.