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Synthesis and Use of a Phosphonate Amidine to Generate an Anti-Phosphoarginine-Specific Antibody

Jakob Fuhrmann1, Venkataraman Subramanian2,3, Paul R Thompson4,5

  • 1Department of Chemistry, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458 (USA). jfuhrman@scripps.edu.

Angewandte Chemie (International Ed. in English)
|October 13, 2015
PubMed

Insights

Researchers developed a novel antibody to detect protein arginine phosphorylation (pArg), a crucial modification in bacteria. This antibody enables new studies into pArg

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Protein arginine phosphorylation (pArg) is a vital post-translational modification (PTM) influencing bacterial processes.
  • The acid lability of pArg has historically hindered its study.
  • Understanding pArg is crucial for bacterial growth and virulence research.

Purpose of the Study:

  • To develop chemical mimics of pArg to overcome stability issues.
  • To generate a high-affinity antibody specific for pArg.
  • To investigate the role of pArg in Bacillus subtilis under oxidative stress.

Main Methods:

  • Synthesized phosphonate and sulfonate amidines as pArg isosteres.
  • Utilized these isosteres as haptens to create a sequence-independent anti-pArg antibody.
  • Applied the antibody to detect pArg in Bacillus subtilis.

Main Results:

  • Successfully developed stable pArg isosteres.
  • Generated the first high-affinity, sequence-independent anti-pArg antibody.
  • Demonstrated that arginine phosphorylation is induced in Bacillus subtilis during oxidative stress.

Conclusions:

  • The novel anti-pArg antibody is a valuable tool for studying arginine phosphorylation.
  • The developed chemistry facilitates the creation of pArg mimetics for enzyme inhibition.
  • This work opens new avenues for exploring the biological roles of pArg in bacteria.
Keywords:
N-phosphorylationantibodieshaptensphosphoargininephosphonate amidine

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