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Sequence homology between HLA-bound cytomegalovirus and human peptides: A potential trigger for alloreactivity.

Identifieur interne : 000C03 ( PubMed/Curation ); précédent : 000C02; suivant : 000C04

Sequence homology between HLA-bound cytomegalovirus and human peptides: A potential trigger for alloreactivity.

Auteurs : Charles E. Hall [États-Unis] ; Vishal N. Koparde [États-Unis] ; Maximilian Jameson-Lee [États-Unis] ; Abdelrhman G. Elnasseh [États-Unis] ; Allison F. Scalora [États-Unis] ; David J. Kobulnicky [États-Unis] ; Myrna G. Serrano [États-Unis] ; Catherine H. Roberts [États-Unis] ; Gregory A. Buck [États-Unis] ; Michael C. Neale [États-Unis] ; Daniel E. Nixon [États-Unis] ; Amir A. Toor [États-Unis]

Source :

PloS one [ 1932-6203 ] ; 2017.

RBID : pubmed:28800601

Descripteurs français

KwdFr :
- Antigènes HLA (), Biologie informatique, Clones cellulaires, Cytomegalovirus (métabolisme), Humains, Lymphocytes T (cytologie), Maladie du greffon contre l'hôte (immunologie), Maladie du greffon contre l'hôte (virologie), Mimétisme moléculaire, Peptides (), Protéines virales (métabolisme), Protéome (métabolisme), Réactions croisées (immunologie), Similitude de séquences d'acides aminés.
MESH :
- cytologie : Lymphocytes T.
- immunologie : Maladie du greffon contre l'hôte, Réactions croisées.
- métabolisme : Cytomegalovirus, Protéines virales, Protéome.
- virologie : Maladie du greffon contre l'hôte.
- Antigènes HLA, Biologie informatique, Clones cellulaires, Humains, Mimétisme moléculaire, Peptides, Similitude de séquences d'acides aminés.

English descriptors

KwdEn :
- Clone Cells, Computational Biology, Cross Reactions (immunology), Cytomegalovirus (metabolism), Graft vs Host Disease (immunology), Graft vs Host Disease (virology), HLA Antigens (chemistry), Humans, Molecular Mimicry, Peptides (chemistry), Proteome (metabolism), Sequence Homology, Amino Acid, T-Lymphocytes (cytology), Viral Proteins (metabolism).
MESH :
- chemical , chemistry : HLA Antigens, Peptides.
- cytology : T-Lymphocytes.
- immunology : Cross Reactions, Graft vs Host Disease.
- metabolism : Cytomegalovirus, Proteome, Viral Proteins.
- virology : Graft vs Host Disease.
- Clone Cells, Computational Biology, Humans, Molecular Mimicry, Sequence Homology, Amino Acid.

Abstract

Human cytomegalovirus (hCMV) reactivation may often coincide with the development of graft-versus-host-disease (GVHD) in stem cell transplantation (SCT). Seventy seven SCT donor-recipient pairs (DRP) (HLA matched unrelated donor (MUD), n = 50; matched related donor (MRD), n = 27) underwent whole exome sequencing to identify single nucleotide polymorphisms (SNPs) generating alloreactive peptide libraries for each DRP (9-mer peptide-HLA complexes); Human CMV CROSS (Cross-Reactive Open Source Sequence) database was compiled from NCBI; HLA class I binding affinity for each DRPs HLA was calculated by NetMHCpan 2.8 and hCMV- derived 9-mers algorithmically compared to the alloreactive peptide-HLA complex libraries. Short consecutive (≥6) amino acid (AA) sequence homology matching hCMV to recipient peptides was considered for HLA-bound-peptide (IC50<500nM) cross reactivity. Of the 70,686 hCMV 9-mers contained within the hCMV CROSS database, an average of 29,658 matched the MRD DRP alloreactive peptides and 52,910 matched MUD DRP peptides (p<0.001). In silico analysis revealed multiple high affinity, immunogenic CMV-Human peptide matches (IC50<500 nM) expressed in GVHD-affected tissue-specific manner. hCMV+GVHD was found in 18 patients, 13 developing hCMV viremia before GVHD onset. Analysis of patients with GVHD identified potential cross reactive peptide expression within affected organs. We propose that hCMV peptide sequence homology with human alloreactive peptides may contribute to the pathophysiology of GVHD.

DOI: 10.1371/journal.pone.0178763
PubMed: 28800601

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<term>Maladie du greffon contre l'hôte (virologie)</term>
<term>Mimétisme moléculaire</term>
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<front><div type="abstract" xml:lang="en">Human cytomegalovirus (hCMV) reactivation may often coincide with the development of graft-versus-host-disease (GVHD) in stem cell transplantation (SCT). Seventy seven SCT donor-recipient pairs (DRP) (HLA matched unrelated donor (MUD), n = 50; matched related donor (MRD), n = 27) underwent whole exome sequencing to identify single nucleotide polymorphisms (SNPs) generating alloreactive peptide libraries for each DRP (9-mer peptide-HLA complexes); Human CMV CROSS (Cross-Reactive Open Source Sequence) database was compiled from NCBI; HLA class I binding affinity for each DRPs HLA was calculated by NetMHCpan 2.8 and hCMV- derived 9-mers algorithmically compared to the alloreactive peptide-HLA complex libraries. Short consecutive (≥6) amino acid (AA) sequence homology matching hCMV to recipient peptides was considered for HLA-bound-peptide (IC50<500nM) cross reactivity. Of the 70,686 hCMV 9-mers contained within the hCMV CROSS database, an average of 29,658 matched the MRD DRP alloreactive peptides and 52,910 matched MUD DRP peptides (p<0.001). In silico analysis revealed multiple high affinity, immunogenic CMV-Human peptide matches (IC50<500 nM) expressed in GVHD-affected tissue-specific manner. hCMV+GVHD was found in 18 patients, 13 developing hCMV viremia before GVHD onset. Analysis of patients with GVHD identified potential cross reactive peptide expression within affected organs. We propose that hCMV peptide sequence homology with human alloreactive peptides may contribute to the pathophysiology of GVHD.</div>
</front>
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<DateCompleted><Year>2017</Year>
<Month>10</Month>
<Day>09</Day>
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<Abstract><AbstractText>Human cytomegalovirus (hCMV) reactivation may often coincide with the development of graft-versus-host-disease (GVHD) in stem cell transplantation (SCT). Seventy seven SCT donor-recipient pairs (DRP) (HLA matched unrelated donor (MUD), n = 50; matched related donor (MRD), n = 27) underwent whole exome sequencing to identify single nucleotide polymorphisms (SNPs) generating alloreactive peptide libraries for each DRP (9-mer peptide-HLA complexes); Human CMV CROSS (Cross-Reactive Open Source Sequence) database was compiled from NCBI; HLA class I binding affinity for each DRPs HLA was calculated by NetMHCpan 2.8 and hCMV- derived 9-mers algorithmically compared to the alloreactive peptide-HLA complex libraries. Short consecutive (≥6) amino acid (AA) sequence homology matching hCMV to recipient peptides was considered for HLA-bound-peptide (IC50<500nM) cross reactivity. Of the 70,686 hCMV 9-mers contained within the hCMV CROSS database, an average of 29,658 matched the MRD DRP alloreactive peptides and 52,910 matched MUD DRP peptides (p<0.001). In silico analysis revealed multiple high affinity, immunogenic CMV-Human peptide matches (IC50<500 nM) expressed in GVHD-affected tissue-specific manner. hCMV+GVHD was found in 18 patients, 13 developing hCMV viremia before GVHD onset. Analysis of patients with GVHD identified potential cross reactive peptide expression within affected organs. We propose that hCMV peptide sequence homology with human alloreactive peptides may contribute to the pathophysiology of GVHD.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hall</LastName>
<ForeName>Charles E</ForeName>
<Initials>CE</Initials>
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<AffiliationInfo><Affiliation>Bone Marrow Transplant Program, Massey Cancer Center, Virginia Commonwealth University, Richmond, Virginia, United States of America.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Koparde</LastName>
<ForeName>Vishal N</ForeName>
<Initials>VN</Initials>
<AffiliationInfo><Affiliation>Center for the Study of Biological Complexity, Virginia Commonwealth University, Richmond, Virginia, United States of America.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Jameson-Lee</LastName>
<ForeName>Maximilian</ForeName>
<Initials>M</Initials>
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Sequence homology between HLA-bound cytomegalovirus and human peptides: A potential trigger for alloreactivity.

Sequence homology between HLA-bound cytomegalovirus and human peptides: A potential trigger for alloreactivity.

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