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PhIP-Seq characterization of serum antibodies using oligonucleotide-encoded peptidomes.
Mohan, Divya; Wansley, Daniel L; Sie, Brandon M; Noon, Muhammad S; Baer, Alan N; Laserson, Uri; Larman, H Benjamin.
Afiliação
  • Mohan D; Division of Immunology, Department of Pathology, Johns Hopkins University, Baltimore, MD, USA.
  • Wansley DL; Division of Immunology, Department of Pathology, Johns Hopkins University, Baltimore, MD, USA.
  • Sie BM; Division of Immunology, Department of Pathology, Johns Hopkins University, Baltimore, MD, USA.
  • Noon MS; Division of Immunology, Department of Pathology, Johns Hopkins University, Baltimore, MD, USA.
  • Baer AN; Division of Rheumatology, Department of Medicine, Johns Hopkins University, Baltimore, MD, USA.
  • Laserson U; Department of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA. uri@lasersonlab.org.
  • Larman HB; Division of Immunology, Department of Pathology, Johns Hopkins University, Baltimore, MD, USA. hlarman1@jhmi.edu.
Nat Protoc ; 13(9): 1958-1978, 2018 09.
Article em En | MEDLINE | ID: mdl-30190553
The binding specificities of an individual's antibody repertoire contain a wealth of biological information. They harbor evidence of environmental exposures, allergies, ongoing or emerging autoimmune disease processes, and responses to immunomodulatory therapies, for example. Highly multiplexed methods to comprehensively interrogate antibody-binding specificities have therefore emerged in recent years as important molecular tools. Here, we provide a detailed protocol for performing 'phage immunoprecipitation sequencing' (PhIP-Seq), which is a powerful method for analyzing antibody-repertoire binding specificities with high throughput and at low cost. The methodology uses oligonucleotide library synthesis (OLS) to encode proteomic-scale peptide libraries for display on bacteriophage. These libraries are then immunoprecipitated, using an individual's antibodies, for subsequent analysis by high-throughput DNA sequencing. We have used PhIP-Seq to identify novel self-antigens associated with autoimmune disease, to characterize the self-reactivity of broadly neutralizing HIV antibodies, and in a large international cross-sectional study of exposure to hundreds of human viruses. Compared with alternative array-based techniques, PhIP-Seq is far more scalable in terms of sample throughput and cost per analysis. Cloning and expression of recombinant proteins are not required (versus protein microarrays), and peptide lengths are limited only by DNA synthesis chemistry (up to 90-aa (amino acid) peptides versus the typical 8- to 12-aa length limit of synthetic peptide arrays). Compared with protein microarrays, however, PhIP-Seq libraries lack discontinuous epitopes and post-translational modifications. To increase the accessibility of PhIP-Seq, we provide detailed instructions for the design of phage-displayed peptidome libraries, their immunoprecipitation using serum antibodies, deep sequencing-based measurement of peptide abundances, and statistical determination of peptide enrichments that reflect antibody-peptide interactions. Once a library has been constructed, PhIP-Seq data can be obtained for analysis within a week.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Análise de Sequência de DNA / Imunoprecipitação / Anticorpos Tipo de estudo: Guideline / Observational_studies / Risk_factors_studies Limite: Humans Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Análise de Sequência de DNA / Imunoprecipitação / Anticorpos Tipo de estudo: Guideline / Observational_studies / Risk_factors_studies Limite: Humans Idioma: En Ano de publicação: 2018 Tipo de documento: Article