Human Leukocyte Antigens A3001 and A3002 Show Distinct Peptide-Binding Patterns of the Mycobacterium tuberculosis Protein TB10.4: Consequences for Immune Recognition

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Published inClinical and Vaccine Immunology Vol. 18; no. 1; pp. 125 - 134
Main Authors Axelsson-Robertson, Rebecca, Ahmed, Raija K., Weichold, Frank F., Ehlers, Marthie M., Kock, Marleen M., Sizemore, Donata, Sadoff, Jerry, Maeurer, Markus
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.01.2011
American Society for Microbiology (ASM)
Subjects
Amino Acid Sequence
Antigens, Bacterial - chemistry
Antigens, Bacterial - genetics
Antigens, Bacterial - immunology
Antigens, Bacterial - metabolism
Binding Sites
CD8-Positive T-Lymphocytes - immunology
Epitopes - genetics
Epitopes - immunology
HLA Antigens - chemistry
HLA Antigens - genetics
HLA Antigens - immunology
HLA Antigens - metabolism
HLA-A Antigens - chemistry
HLA-A Antigens - genetics
HLA-A Antigens - immunology
HLA-A Antigens - metabolism
Humans
Microbial Immunology
Molecular Sequence Data
Mycobacterium tuberculosis
Peptide Library
Peptides - chemistry
Peptides - immunology
Peptides - metabolism
Protein Binding
South Africa
Tuberculosis, Pulmonary - immunology
South Africa
Online AccessGet full text
ISSN1556-6811
1556-679X
1556-679X
DOI10.1128/CVI.00302-10

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Abstract Classifications Services CVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue CVI About CVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy CVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 1556-6811 Online ISSN: 1556-679X Copyright © 2014 by the American Society for Microbiology.   For an alternate route to CVI .asm.org, visit: CVI       
AbstractList High-tuberculosis (TB)-burden countries are located in sub-Saharan Africa. We examined the frequency of human leukocyte antigen (HLA) alleles, followed by recombinant expression of the most frequent HLA-A alleles, i.e., HLA-A*3001 and HLA-A*3002, to study differences in mycobacterial peptide presentation and CD8+ T-cell recognition. We screened a peptide library (9-mer peptides with an 8-amino-acid overlap) for binding, affinity, and off-rate of the Mycobacterium tuberculosis-associated antigen TB10.4 and identified only three TB10.4 peptides with considerable binding to HLA-A*3001. In contrast, 22 peptides bound to HLA-A*3002. This reflects a marked difference in the binding preference between the two alleles, with A*3002 tolerating a more promiscuous peptide-binding pattern and A*3001 accommodating only a very selective peptide repertoire. Subsequent analysis of the affinity and off-rate of the binding peptides revealed a strong affinity (8 nM to 7 mu M) and moderate off-rate (20 min to 3 h) for both alleles. Construction of HLA-A*3001 and HLA-A*3002 tetramers containing selected binding peptides from TB10.4, including a peptide which was shared among both alleles, QIMYNYPAM (TB10.43-11), allowed us to enumerate epitope-specific T cells in HLA-A*3001- and HLA-A*3002-typed patients with active TB. HLA-A*3001 and HLA-A*3002 major histocompatibility complex-peptide complexes were recognized in individuals with active TB, irrespective of their homozygous HLA-A*3001 or HLA-A*3002 genetic background. The antigen-specific T cells exhibited the CD45RA+ CCR7+ precursor phenotype and the interleukin-7 receptor (CD127), which were different from the phenotype and receptor exhibited by the parental CD8+ T-cell population.
Classifications Services CVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue CVI About CVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy CVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 1556-6811 Online ISSN: 1556-679X Copyright © 2014 by the American Society for Microbiology.   For an alternate route to CVI .asm.org, visit: CVI       
High-tuberculosis (TB)-burden countries are located in sub-Saharan Africa. We examined the frequency of human leukocyte antigen (HLA) alleles, followed by recombinant expression of the most frequent HLA-A alleles, i.e., HLA-A*3001 and HLA-A*3002, to study differences in mycobacterial peptide presentation and CD8 + T-cell recognition. We screened a peptide library (9-mer peptides with an 8-amino-acid overlap) for binding, affinity, and off-rate of the Mycobacterium tuberculosis -associated antigen TB10.4 and identified only three TB10.4 peptides with considerable binding to HLA-A*3001. In contrast, 22 peptides bound to HLA-A*3002. This reflects a marked difference in the binding preference between the two alleles, with A*3002 tolerating a more promiscuous peptide-binding pattern and A*3001 accommodating only a very selective peptide repertoire. Subsequent analysis of the affinity and off-rate of the binding peptides revealed a strong affinity (8 nM to 7 μM) and moderate off-rate (20 min to 3 h) for both alleles. Construction of HLA-A*3001 and HLA-A*3002 tetramers containing selected binding peptides from TB10.4, including a peptide which was shared among both alleles, QIMYNYPAM (TB10.4 3-11 ), allowed us to enumerate epitope-specific T cells in HLA-A*3001- and HLA-A*3002-typed patients with active TB. HLA-A*3001 and HLA-A*3002 major histocompatibility complex-peptide complexes were recognized in individuals with active TB, irrespective of their homozygous HLA-A*3001 or HLA-A*3002 genetic background. The antigen-specific T cells exhibited the CD45RA + CCR7 + precursor phenotype and the interleukin-7 receptor (CD127), which were different from the phenotype and receptor exhibited by the parental CD8 + T-cell population.
High-tuberculosis (TB)-burden countries are located in sub-Saharan Africa. We examined the frequency of human leukocyte antigen (HLA) alleles, followed by recombinant expression of the most frequent HLA-A alleles, i.e., HLA-A*3001 and HLA-A*3002, to study differences in mycobacterial peptide presentation and CD8(+) T-cell recognition. We screened a peptide library (9-mer peptides with an 8-amino-acid overlap) for binding, affinity, and off-rate of the Mycobacterium tuberculosis-associated antigen TB10.4 and identified only three TB10.4 peptides with considerable binding to HLA-A*3001. In contrast, 22 peptides bound to HLA-A*3002. This reflects a marked difference in the binding preference between the two alleles, with A*3002 tolerating a more promiscuous peptide-binding pattern and A*3001 accommodating only a very selective peptide repertoire. Subsequent analysis of the affinity and off-rate of the binding peptides revealed a strong affinity (8 nM to 7 μM) and moderate off-rate (20 min to 3 h) for both alleles. Construction of HLA-A*3001 and HLA-A*3002 tetramers containing selected binding peptides from TB10.4, including a peptide which was shared among both alleles, QIMYNYPAM (TB10.4(3-11)), allowed us to enumerate epitope-specific T cells in HLA-A*3001- and HLA-A*3002-typed patients with active TB. HLA-A*3001 and HLA-A*3002 major histocompatibility complex-peptide complexes were recognized in individuals with active TB, irrespective of their homozygous HLA-A*3001 or HLA-A*3002 genetic background. The antigen-specific T cells exhibited the CD45RA(+) CCR7(+) precursor phenotype and the interleukin-7 receptor (CD127), which were different from the phenotype and receptor exhibited by the parental CD8(+) T-cell population.
High-tuberculosis (TB)-burden countries are located in sub-Saharan Africa. We examined the frequency of human leukocyte antigen (HLA) alleles, followed by recombinant expression of the most frequent HLA-A alleles, i.e., HLA-A*3001 and HLA-A*3002, to study differences in mycobacterial peptide presentation and CD8(+) T-cell recognition. We screened a peptide library (9-mer peptides with an 8-amino-acid overlap) for binding, affinity, and off-rate of the Mycobacterium tuberculosis-associated antigen TB10.4 and identified only three TB10.4 peptides with considerable binding to HLA-A*3001. In contrast, 22 peptides bound to HLA-A*3002. This reflects a marked difference in the binding preference between the two alleles, with A*3002 tolerating a more promiscuous peptide-binding pattern and A*3001 accommodating only a very selective peptide repertoire. Subsequent analysis of the affinity and off-rate of the binding peptides revealed a strong affinity (8 nM to 7 μM) and moderate off-rate (20 min to 3 h) for both alleles. Construction of HLA-A*3001 and HLA-A*3002 tetramers containing selected binding peptides from TB10.4, including a peptide which was shared among both alleles, QIMYNYPAM (TB10.4(3-11)), allowed us to enumerate epitope-specific T cells in HLA-A*3001- and HLA-A*3002-typed patients with active TB. HLA-A*3001 and HLA-A*3002 major histocompatibility complex-peptide complexes were recognized in individuals with active TB, irrespective of their homozygous HLA-A*3001 or HLA-A*3002 genetic background. The antigen-specific T cells exhibited the CD45RA(+) CCR7(+) precursor phenotype and the interleukin-7 receptor (CD127), which were different from the phenotype and receptor exhibited by the parental CD8(+) T-cell population.High-tuberculosis (TB)-burden countries are located in sub-Saharan Africa. We examined the frequency of human leukocyte antigen (HLA) alleles, followed by recombinant expression of the most frequent HLA-A alleles, i.e., HLA-A*3001 and HLA-A*3002, to study differences in mycobacterial peptide presentation and CD8(+) T-cell recognition. We screened a peptide library (9-mer peptides with an 8-amino-acid overlap) for binding, affinity, and off-rate of the Mycobacterium tuberculosis-associated antigen TB10.4 and identified only three TB10.4 peptides with considerable binding to HLA-A*3001. In contrast, 22 peptides bound to HLA-A*3002. This reflects a marked difference in the binding preference between the two alleles, with A*3002 tolerating a more promiscuous peptide-binding pattern and A*3001 accommodating only a very selective peptide repertoire. Subsequent analysis of the affinity and off-rate of the binding peptides revealed a strong affinity (8 nM to 7 μM) and moderate off-rate (20 min to 3 h) for both alleles. Construction of HLA-A*3001 and HLA-A*3002 tetramers containing selected binding peptides from TB10.4, including a peptide which was shared among both alleles, QIMYNYPAM (TB10.4(3-11)), allowed us to enumerate epitope-specific T cells in HLA-A*3001- and HLA-A*3002-typed patients with active TB. HLA-A*3001 and HLA-A*3002 major histocompatibility complex-peptide complexes were recognized in individuals with active TB, irrespective of their homozygous HLA-A*3001 or HLA-A*3002 genetic background. The antigen-specific T cells exhibited the CD45RA(+) CCR7(+) precursor phenotype and the interleukin-7 receptor (CD127), which were different from the phenotype and receptor exhibited by the parental CD8(+) T-cell population.
Author Raija K. Ahmed
Marleen M. Kock
Frank F. Weichold
Marthie M. Ehlers
Rebecca Axelsson-Robertson
Donata Sizemore
Markus Maeurer
Jerry Sadoff
AuthorAffiliation Department of Microbiology, Tumor and Cell Biology, Karolinska Institute, Stockholm, Sweden, 1 Swedish Institute for Infectious Disease Control, Stockholm, Sweden, 2 Aeras Global TB Vaccine Foundation, Rockville, Maryland, 3 Department of Medical Microbiology, University of Pretoria/NHLS, Pretoria, South Africa 4
AuthorAffiliation_xml – name: Department of Microbiology, Tumor and Cell Biology, Karolinska Institute, Stockholm, Sweden, 1 Swedish Institute for Infectious Disease Control, Stockholm, Sweden, 2 Aeras Global TB Vaccine Foundation, Rockville, Maryland, 3 Department of Medical Microbiology, University of Pretoria/NHLS, Pretoria, South Africa 4
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  organization: Department of Microbiology, Tumor and Cell Biology, Karolinska Institute, Stockholm, Sweden, Swedish Institute for Infectious Disease Control, Stockholm, Sweden, Aeras Global TB Vaccine Foundation, Rockville, Maryland, Department of Medical Microbiology, University of Pretoria/NHLS, Pretoria, South Africa
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  givenname: Raija K.
  surname: Ahmed
  fullname: Ahmed, Raija K.
  organization: Department of Microbiology, Tumor and Cell Biology, Karolinska Institute, Stockholm, Sweden, Swedish Institute for Infectious Disease Control, Stockholm, Sweden, Aeras Global TB Vaccine Foundation, Rockville, Maryland, Department of Medical Microbiology, University of Pretoria/NHLS, Pretoria, South Africa
– sequence: 3
  givenname: Frank F.
  surname: Weichold
  fullname: Weichold, Frank F.
  organization: Department of Microbiology, Tumor and Cell Biology, Karolinska Institute, Stockholm, Sweden, Swedish Institute for Infectious Disease Control, Stockholm, Sweden, Aeras Global TB Vaccine Foundation, Rockville, Maryland, Department of Medical Microbiology, University of Pretoria/NHLS, Pretoria, South Africa
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  surname: Kock
  fullname: Kock, Marleen M.
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  surname: Sizemore
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  organization: Department of Microbiology, Tumor and Cell Biology, Karolinska Institute, Stockholm, Sweden, Swedish Institute for Infectious Disease Control, Stockholm, Sweden, Aeras Global TB Vaccine Foundation, Rockville, Maryland, Department of Medical Microbiology, University of Pretoria/NHLS, Pretoria, South Africa
– sequence: 7
  givenname: Jerry
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  fullname: Sadoff, Jerry
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High-tuberculosis (TB)-burden countries are located in sub-Saharan Africa. We examined the frequency of human leukocyte antigen (HLA) alleles, followed by...
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SubjectTerms Amino Acid Sequence
Antigens, Bacterial - chemistry
Antigens, Bacterial - genetics
Antigens, Bacterial - immunology
Antigens, Bacterial - metabolism
Binding Sites
CD8-Positive T-Lymphocytes - immunology
Epitopes - genetics
Epitopes - immunology
HLA Antigens - chemistry
HLA Antigens - genetics
HLA Antigens - immunology
HLA Antigens - metabolism
HLA-A Antigens - chemistry
HLA-A Antigens - genetics
HLA-A Antigens - immunology
HLA-A Antigens - metabolism
Humans
Microbial Immunology
Molecular Sequence Data
Mycobacterium tuberculosis
Peptide Library
Peptides - chemistry
Peptides - immunology
Peptides - metabolism
Protein Binding
South Africa
Tuberculosis, Pulmonary - immunology
Title Human Leukocyte Antigens A3001 and A3002 Show Distinct Peptide-Binding Patterns of the Mycobacterium tuberculosis Protein TB10.4: Consequences for Immune Recognition
URI http://cvi.asm.org/content/18/1/125.abstract
https://www.ncbi.nlm.nih.gov/pubmed/21084459
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