Histamine binding activity of surface-modified yeast by histamine binding protein (HBP)

Hyeweon Jang1, Geun Woo Lee1, Yang-Hoon Kim2

  • 1Graduate School of Semiconductor and Chemical Engineering, Jeonbuk National University, 567 Baekje-daero, Deokjin-gu, 54896, Jeonju-si, Jeollabuk-do, Republic of Korea.

AMB Express
|October 30, 2021
PubMed

Insights

This study engineered yeast to display a mite

Area of Science:

  • Immunology
  • Biotechnology

Background:

  • Histamine is a key immune mediator; excessive levels or poor degradation cause adverse effects.
  • Histamine binding protein (HBP) from mites binds histamine to suppress host immune responses.

Purpose of the Study:

  • To express recombinant HBP on yeast surfaces (MBTL-GWL-1).
  • To evaluate the histamine inhibitory capacity of engineered yeast cells.

Main Methods:

  • Cloning HBP into yeast for surface expression.
  • Confirmation of recombinant protein expression using immunofluorescence and Western blot.
  • Assessing histamine inhibition by GWL-1 cells in a dose-dependent manner.
  • Phagocytosis assays using RAW 264.7 cells to confirm histamine capture.

Main Results:

  • Recombinant HBP was successfully expressed on the yeast surface (GWL-1).
  • GWL-1 cells demonstrated significant histamine inhibitory ability (up to 60% at 1.30 × 107 CFU/ml).
  • Histamine inhibition was dose-dependent on GWL-1 cell concentration.
  • Both whole and dead GWL-1 cells showed histamine inhibitory effects, with whole cells being more effective.
  • Phagocytosis assays confirmed that GWL-1 cells capture histamine.

Conclusions:

  • Engineered yeast (GWL-1) effectively binds and inhibits histamine.
  • This system shows potential as a novel anti-allergy therapeutic material.