AustralieFrV1, PubMed, Checkpoint, bibRecord, 000751

Natural immune response to Plasmodium vivax alpha-helical coiled coil protein motifs and its association with the risk of P. vivax malaria.

Identifieur interne : 000751 ( PubMed/Checkpoint ); précédent : 000750; suivant : 000752

Natural immune response to Plasmodium vivax alpha-helical coiled coil protein motifs and its association with the risk of P. vivax malaria.

Auteurs : Nora Céspedes [Colombie] ; Connie S N. Li Wai Suen [Australie] ; Cristian Koepfli [Australie] ; Camila T. França [Australie] ; Ingrid Felger [Suisse] ; Issa Nebie [Burkina Faso] ; Myriam Arévalo-Herrera [Colombie] ; Ivo Mueller [Australie] ; Giampietro Corradin [Suisse] ; S Crates Herrera [Colombie]

Source :

PloS one [ 1932-6203 ] ; 2017.

RBID : pubmed:28651021

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Protozoan (blood), Antigens, Protozoan (chemistry), Antigens, Protozoan (genetics), Child, Preschool, Humans, Immunity, Innate, Immunoglobulin G (blood), Infant, Longitudinal Studies, Malaria Vaccines (genetics), Malaria Vaccines (immunology), Malaria, Vivax (immunology), Malaria, Vivax (parasitology), Malaria, Vivax (prevention & control), Papua New Guinea, Peptides (chemistry), Peptides (genetics), Peptides (immunology), Plasmodium vivax (chemistry), Plasmodium vivax (genetics), Plasmodium vivax (immunology), Protein Conformation, alpha-Helical, Protozoan Proteins (chemistry), Protozoan Proteins (genetics), Protozoan Proteins (immunology), Risk Factors.
MESH :
- chemical , blood : Antibodies, Protozoan, Immunoglobulin G.
- chemical , chemistry : Antigens, Protozoan, Peptides, Protozoan Proteins.
- chemical , genetics : Antigens, Protozoan, Malaria Vaccines, Peptides, Protozoan Proteins.
- chemical , immunology : Malaria Vaccines, Peptides, Protozoan Proteins.
- chemistry : Plasmodium vivax.
- genetics : Plasmodium vivax.
- immunology : Malaria, Vivax, Plasmodium vivax.
- parasitology : Malaria, Vivax.
- prevention & control : Malaria, Vivax.
- Amino Acid Sequence, Animals, Child, Preschool, Humans, Immunity, Innate, Infant, Longitudinal Studies, Papua New Guinea, Protein Conformation, alpha-Helical, Risk Factors.

Abstract

Protein α-helical coiled coil structures are known to induce antibodies able to block critical functions in different pathogens. In a previous study, a total of 50 proteins of Plasmodium vivax erythrocytic asexual stages containing α-helical coiled coil structural motifs were identified in silico, and the corresponding peptides were chemically synthesized. A total of 43 peptides were recognized by naturally acquired antibodies in plasma samples from both Papua New Guinea (PNG) and Colombian adult donors. In this study, the association between IgG antibodies to these peptides and clinical immunity was further explored by measuring total IgG antibody levels to 24 peptides in baseline samples from a longitudinal study of children aged 1-3 years (n = 164) followed for 16 months. Samples were reactive to all peptides tested. Eight peptides were recognized by >50% of individuals, whereas only one peptide had < 20% reactivity. Children infected at baseline were seropositive to 23/24 peptides. No significant association was observed between antibody titers and age or molecular force of infection, suggesting that antibody levels had already reached an equilibrium. There was a strong association between antibody levels to all peptides and protection against P. vivax clinical episodes during the 16 months follow-up. These results suggest that the selected coiled coil antigens might be good markers of both exposure and acquired immunity to P. vivax malaria, and further preclinical investigation should be performed to determine their potential as P. vivax vaccine antigens.

DOI: 10.1371/journal.pone.0179863
PubMed: 28651021

Affiliations:

Australie, Burkina Faso, Colombie, Suisse

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Le document en format XML

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<term>Antigens, Protozoan (chemistry)</term>
<term>Antigens, Protozoan (genetics)</term>
<term>Child, Preschool</term>
<term>Humans</term>
<term>Immunity, Innate</term>
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<term>Peptides (immunology)</term>
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<term>Plasmodium vivax (genetics)</term>
<term>Plasmodium vivax (immunology)</term>
<term>Protein Conformation, alpha-Helical</term>
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<term>Protéines de protozoaire</term>
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<front><div type="abstract" xml:lang="en">Protein α-helical coiled coil structures are known to induce antibodies able to block critical functions in different pathogens. In a previous study, a total of 50 proteins of Plasmodium vivax erythrocytic asexual stages containing α-helical coiled coil structural motifs were identified in silico, and the corresponding peptides were chemically synthesized. A total of 43 peptides were recognized by naturally acquired antibodies in plasma samples from both Papua New Guinea (PNG) and Colombian adult donors. In this study, the association between IgG antibodies to these peptides and clinical immunity was further explored by measuring total IgG antibody levels to 24 peptides in baseline samples from a longitudinal study of children aged 1-3 years (n = 164) followed for 16 months. Samples were reactive to all peptides tested. Eight peptides were recognized by >50% of individuals, whereas only one peptide had < 20% reactivity. Children infected at baseline were seropositive to 23/24 peptides. No significant association was observed between antibody titers and age or molecular force of infection, suggesting that antibody levels had already reached an equilibrium. There was a strong association between antibody levels to all peptides and protection against P. vivax clinical episodes during the 16 months follow-up. These results suggest that the selected coiled coil antigens might be good markers of both exposure and acquired immunity to P. vivax malaria, and further preclinical investigation should be performed to determine their potential as P. vivax vaccine antigens.</div>
</front>
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<Abstract><AbstractText>Protein α-helical coiled coil structures are known to induce antibodies able to block critical functions in different pathogens. In a previous study, a total of 50 proteins of Plasmodium vivax erythrocytic asexual stages containing α-helical coiled coil structural motifs were identified in silico, and the corresponding peptides were chemically synthesized. A total of 43 peptides were recognized by naturally acquired antibodies in plasma samples from both Papua New Guinea (PNG) and Colombian adult donors. In this study, the association between IgG antibodies to these peptides and clinical immunity was further explored by measuring total IgG antibody levels to 24 peptides in baseline samples from a longitudinal study of children aged 1-3 years (n = 164) followed for 16 months. Samples were reactive to all peptides tested. Eight peptides were recognized by >50% of individuals, whereas only one peptide had < 20% reactivity. Children infected at baseline were seropositive to 23/24 peptides. No significant association was observed between antibody titers and age or molecular force of infection, suggesting that antibody levels had already reached an equilibrium. There was a strong association between antibody levels to all peptides and protection against P. vivax clinical episodes during the 16 months follow-up. These results suggest that the selected coiled coil antigens might be good markers of both exposure and acquired immunity to P. vivax malaria, and further preclinical investigation should be performed to determine their potential as P. vivax vaccine antigens.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Céspedes</LastName>
<ForeName>Nora</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Malaria Vaccine and Drug Development Center (MVDC), Cali, Colombia.</Affiliation>
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<AffiliationInfo><Affiliation>School of Health, University of Valle, Cali, Colombia.</Affiliation>
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<AffiliationInfo><Affiliation>Department of Medical Biology, University of Melbourne, Melbourne, Australia.</Affiliation>
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<AffiliationInfo><Affiliation>Department of Medical Biology, University of Melbourne, Melbourne, Australia.</Affiliation>
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<Initials>CT</Initials>
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<AffiliationInfo><Affiliation>Department of Medical Biology, University of Melbourne, Melbourne, Australia.</Affiliation>
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<Initials>I</Initials>
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<Initials>I</Initials>
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<Initials>M</Initials>
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<AffiliationInfo><Affiliation>School of Health, University of Valle, Cali, Colombia.</Affiliation>
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<Author ValidYN="Y"><LastName>Mueller</LastName>
<ForeName>Ivo</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>Population Health & Immunity Division, Walter and Eliza Hall Institute of Medical Research, Parkville, Australia.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Medical Biology, University of Melbourne, Melbourne, Australia.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Malaria: Parasites and Hosts Unit, Department of Parasites & Insect Vectors, Institut Pasteur, Paris, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Barcelona Institute of Global Health (ISGLOBAL), Barcelona, Spain.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Corradin</LastName>
<ForeName>Giampietro</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Biochemistry Department, University of Lausanne, Epalinges, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Herrera</LastName>
<ForeName>Sócrates</ForeName>
<Initials>S</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0002-4688-0598</Identifier>
<AffiliationInfo><Affiliation>Malaria Vaccine and Drug Development Center (MVDC), Cali, Colombia.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Caucaseco Scientific Research Center, Cali, Colombia.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>U19 AI089702</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
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<Month>06</Month>
<Day>26</Day>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000913" MajorTopicYN="N">Antibodies, Protozoan</DescriptorName>
<QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName>
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<MeshHeading><DescriptorName UI="D000953" MajorTopicYN="N">Antigens, Protozoan</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
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<MeshHeading><DescriptorName UI="D002675" MajorTopicYN="N">Child, Preschool</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007113" MajorTopicYN="N">Immunity, Innate</DescriptorName>
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<MeshHeading><DescriptorName UI="D008137" MajorTopicYN="N">Longitudinal Studies</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017780" MajorTopicYN="N">Malaria Vaccines</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016780" MajorTopicYN="N">Malaria, Vivax</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName>
<QualifierName UI="Q000517" MajorTopicYN="N">prevention & control</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010219" MajorTopicYN="N">Papua New Guinea</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010966" MajorTopicYN="N">Plasmodium vivax</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072756" MajorTopicYN="N">Protein Conformation, alpha-Helical</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015800" MajorTopicYN="N">Protozoan Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012307" MajorTopicYN="N">Risk Factors</DescriptorName>
</MeshHeading>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>03</Month>
<Day>15</Day>
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<Month>06</Month>
<Day>05</Day>
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<affiliations><list><country><li>Australie</li>
<li>Burkina Faso</li>
<li>Colombie</li>
<li>Suisse</li>
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<name sortKey="Franca, Camila T" sort="Franca, Camila T" uniqKey="Franca C" first="Camila T" last="França">Camila T. França</name>
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<name sortKey="Corradin, Giampietro" sort="Corradin, Giampietro" uniqKey="Corradin G" first="Giampietro" last="Corradin">Giampietro Corradin</name>
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<country name="Burkina Faso"><noRegion><name sortKey="Nebie, Issa" sort="Nebie, Issa" uniqKey="Nebie I" first="Issa" last="Nebie">Issa Nebie</name>
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Natural immune response to Plasmodium vivax alpha-helical coiled coil protein motifs and its association with the risk of P. vivax malaria.

Natural immune response to Plasmodium vivax alpha-helical coiled coil protein motifs and its association with the risk of P. vivax malaria.

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