Human recombinant Fab fragments with sub-nanomolar affinities for acetylated histones

Iglika Batova, Czeslawa Kowal, Rena May, Matthew D. Scharff, Betty Diamond

Research output: Contribution to journalReview article

3 Scopus citations

Abstract

Acetylation of lysines at different sites in the N-terminus of core histones is a common mode of chromatin modification; different combinations of such modifications are associated with distinct patterns of gene expression, replication and repair. Antibodies are usually used to identify and localize particular histone modifications and to correlate their presence with transcription or other cellular processes. This requires antibodies of sufficient specificity and affinity for each of the many modifications that have now been observed. In most instances, polyclonal antibodies have been used but monoclonal antibodies can also be effective. Here we report that a phage-displayed repertoire of rearranged antibody genes from splenic B cells from a patient with systemic lupus contain Fab fragments that can bind native acetylated lysine 8 histone H4. This finding represents the first selection of human antibodies specific for acetylated histone and suggests that lupus antibodies may contribute to dissection of the histone code.

Original languageEnglish (US)
Pages (from-to)1-10
Number of pages10
JournalJournal of Immunological Methods
Volume329
Issue number1-2
DOIs
StatePublished - Jan 1 2008

Keywords

  • Acetylated histones
  • Combinatorial library
  • Immunoprecipitation
  • Monoclonal antibodies
  • SLE

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint Dive into the research topics of 'Human recombinant Fab fragments with sub-nanomolar affinities for acetylated histones'. Together they form a unique fingerprint.

  • Cite this