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Updated: Oct 15, 2025

Protein Engineering by Yeast Surface Display
Published on: November 29, 2024
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.
Abstract:
Histamine is an immune mediator that is mainly secreted when an immediate, rapid response is needed in the body, and an excessive secretion of histamine or lack of enzymes that degrade histamine can result in various side effects. Histamine binding protein (HBP) is secreted by a mite species to prevent the host's histamine-induced immune responses by binding the histamine molecule in the blood. Cloning was performed to express HBP on the yeast surface (MBTL-GWL-1), and immunofluorescence (IF) and western blot was performed to confirm the expression of the recombinant protein. The histamine inhibitory ability of GWL-1 cells was tested according to the cell concentration. The highest inhibitory ability of 1.30 × 107 CFU/ml of GWL-1 cells was of about 60 %. The GWL-1 cell concentration and the degree of histamine inhibition were confirmed to be dose-dependent, and dead cell debris was shown to have a histamine inhibitory effect, although not as much as that of whole cells. Phagocytosis assays were performed to determine whether histamine affected the RAW 264.7 cell's phagocytosis, and to indirectly confirm the GWL-1 cell's histamine inhibition. By confirming that, we found that GWL-1 captures histamine. Therefore, it can be expected to become a competitive material in the anti-allergy market.
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.

