Evidence map›Paper›PMID 25706099›Full record

ArticlePathogens and global health2015

In silico analysis for structure, function and T-cell epitopes of a hypothetical conserved (HP-C) protein coded by PVX_092425 in Plasmodium vivax.

Jinyu Mo, Jian Li

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Article in Pathogens and global health, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Jinyu Mo
Jian Li
Hubei University of Medicine · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivePlasmodium spp. merozoite glycosylphosphatidylinositol-anchored proteins (GPI-APs) considered as protective immunogen in novel vaccines against malaria. To analyze the structure and function of a hypothetical conserved (HP-C) GPI-AP coded by gene PVX_092425 from Plasmodium vivax, and find its potential T-cell epitopes for further vivax malaria vaccine study.

methodsThe structure, function and T-cell epitopes of the HP-C protein named Pvx_092425 were analyzed and predicted by online and offline bioinformatics software.

resultsThe bioinformatics data showed that the Pvx_092425 is an 830 amino acid (AA) long polypeptide encoded by five exons gene PVX_092425.It contains a pectin lyase-like superfamily, an AA repeats region, a cys-rich region and a transmembrane domain (TM) in C-terminal region. The alignment analysis drew it has a unique AA repeats region among Plasmodium spp. It was located in the cytoplasm, secretory system or cellular nucleus of P. vivax merozoite. For the sequence, the fragment of I823-V829 inserts in the interior side of the membrane, and M1--A812 belongs to the cytoplasmic tail. It has seven protein-protein binding sites. The peptides with the best predicted binding affinities were human leucocyte antigen (HLA) HLA-A*0203, HLA-DRB1*0101 and HLA- DRB1*0701.Among these predicted peptides, 582FLWDKALFD590 epitope interacted with HLA-DRB1*0101 allele showed best binding affinity compared to others. Structural analysis explained that the epitope fits well into the epitope-binding groove of HLA-DRB1*0101.

conclusionsIt proposes that the Pvx_092425 plays a key role during erythrocyte stage and generates information that is useful for development of blood-stage vaccine to block the merozoites invasion.

Indexed as

Amino Acid SequenceAnimalsAntibodies, ProtozoanAntigens, ProtozoanComputational BiologyComputer SimulationEpitopes, T-LymphocyteErythrocytesHost-Parasite InteractionsHumansMalaria, VivaxMembrane ProteinsMerozoite Surface Protein 1Plasmodium vivaxProtein BindingProtozoan ProteinsAntibodies, ProtozoanAntigens, ProtozoanEpitopes, T-LymphocyteMembrane ProteinsMerozoite Surface Protein 1Protozoan ProteinsGlycosylphosphatidylinositol,Human leucocyte antigen,Hypothetical conserved,Molecular docking,Plasmodium vivax,T-cell epitope

Identifiers

PMID25706099
PMCPMC4571820
OpenAlexW1986644572

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.