The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation: The HyHEL-10-HEL interaction

Akiko Yokota, Kouhei Tsumoto, Mitsunori Shiroishi, Hidemasa Kondo, Izumi Kumagai

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

To study the role of hydrogen bonding via interfacial water molecules in protein-protein interactions, we examined the interaction between hen egg white lysozyme (HEL) and its HyHEL-10 variable domain fragment (Fv) antibody. We constructed three antibody mutants (L-Y50F, L-S91A, and L-S93A) and investigated the interactions between the mutant Fvs and HEL. Isothermal titration calorimetry indicated that the mutations significantly decreased the negative enthalpy change (8-25 kJ mol-1), despite some offset by a favorable entropy change. X-ray crystallography demonstrated that the complexes had nearly identical structures, including the positions of the interfacial water molecules. Taken together, the isothermal titration calorimetric and x-ray crystallographic results indicate that hydrogen bonding via interfacial water enthalpically contributes to the Fv-HEL interaction despite the partial offset because of entropy loss, suggesting that hydrogen bonding stiffens the antigen-antibody complex.

Original languageEnglish
Pages (from-to)5410-5418
Number of pages9
JournalJournal of Biological Chemistry
Volume278
Issue number7
DOIs
Publication statusPublished - Feb 14 2003

All Science Journal Classification (ASJC) codes

  • Biochemistry

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