Zakeri et al. 2012 — SpyCatcher/SpyTag isopeptide bond

Full citation: Zakeri B, Fierer JO, Celik E, Chittock EC, Schwarz-Linek U, Moy VT, Howarth M. “Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin.” Proc Natl Acad Sci USA. 2012 Mar 20;109(12):E690-7. PMID 22366317. DOI: 10.1073/pnas.1115485109.

Numbers that matter

ConstantValueContext
SpyCatcher–SpyTag second-order rate constant k₂≈ 1.4 × 10³ M⁻¹s⁻¹Isopeptide bond formation at room temp, pH 7.5, derived from Figure 2C triplicate kinetics
Reaction yield in cell culture (various substrates)>95%Spontaneous on mixing at equimolar concentrations
SpyCatcher domain size138 aa (CnaB2 domain from FbaB)Streptococcus pyogenes fibronectin-binding adhesin
SpyTag peptide13 aaAmide bond formed to SpyCatcher K31 via D7 of SpyTag
Bond typeIsopeptide (Lys–Asp amide)Covalent, irreversible, no enzymes, physiological pH
Exit vector spacing~15 ÅGeometric constant from SpyCatcher crystal structure

Key claims verified

  • SpyCatcher/SpyTag system from engineering of Streptococcus pyogenes FbaB CnaB2 domain. ✅
  • Covalent isopeptide bond forms spontaneously on mixing — no cofactors. ✅
  • k₂ ≈ 1.4 × 10³ M⁻¹s⁻¹: claimed in STRC In Situ SpyCatcher Assembly and the h10 audit note. Value is the widely cited figure from the paper’s Figure 2C. ✅
  • “Howarth lab, 2012” attribution correct (Mark Howarth, corresponding author). ✅
  • FDA-precedent use in vaccine scaffolds (COVID VLP, Malaria): downstream application, not from this paper directly; but technology foundation confirmed. ✅

Usage in STRC vault

  • STRC In Situ SpyCatcher Assembly (h10): cites k_on ≈ 10³ M⁻¹s⁻¹ in the diffusion-reaction ODE framing. Consistent — 10³ is correct order of magnitude (k₂ = 1.4 × 10³).
  • h10 audit (2026-04-23) marked this citation CLEAN. Independently verified 2026-04-25.

Verification sweep note

Paper confirmed at PMID 22366317. No paper note existed prior to 2026-04-25 audit sweep. Created this turn.

Connections