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Human lysozyme (HL) binds to Klebsiella pneumoniae O1 lipopolysaccharide (LPS) via specific residues. This interaction reveals a novel glycan-guided mechanism for bacterial cell wall recognition by lysozyme.

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Area of Science:

  • Structural biology
  • Immunology
  • Microbiology

Background:

  • Human lysozyme (HL) plays a role in innate immunity.
  • Lipopolysaccharide (LPS) from Klebsiella pneumoniae O1 is a key component of this bacterium, often causing lung infections.
  • Understanding HL-LPS interactions is crucial for developing new therapeutic strategies against bacterial infections.

Purpose of the Study:

  • To elucidate the molecular mechanism of interaction between human lysozyme (HL) and Klebsiella pneumoniae O1 LPS.
  • To characterize the binding sites and structural changes involved in HL-LPS recognition.

Main Methods:

  • Surface plasmon resonance (SPR) to detect HL-LPS interactions.
  • Nuclear magnetic resonance (NMR) spectroscopy to study pH-dependent structural rearrangements of HL.
  • X-ray crystallography to determine the high-resolution structure of the HL-tetrasaccharide complex.

Main Results:

  • HL binding to synthetic LPS fragments (disaccharides and tetrasaccharides) was confirmed.
  • NMR revealed pH-dependent structural changes in HL upon disaccharide binding.
  • Crystal structure showed LPS tetrasaccharide chains packing into HL's A, B, C, and D sites via hydrogen bonds and hydrophobic contacts, highlighting the role of specific residues (Glu35, Asp53, Trp63, Asp102).

Conclusions:

  • The study identified specific residues crucial for HL binding to the LPS tetrasaccharide.
  • A novel glycan-guided mechanism for bacterial cell wall recognition by lysozyme was proposed.
  • These findings suggest a potential complementary role for HL in bacterial immune defense.