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Codon Usage in Signal Sequences Affects Protein Expression and Secretion Using Baculovirus/Insect Cell Expression

Yalan Wang1, Yuanhui Mao1,2, Xiaodong Xu1

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Summary

Altering signal peptide sequences impacts protein production in insect cells. Introducing non-optimal codons in FibHsp signal peptides enhanced protein secretion, offering a new strategy for protein expression.

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Area of Science:

  • Molecular Biology
  • Biotechnology
  • Protein Engineering

Background:

  • Signal peptides are crucial for protein secretion.
  • Codon usage and mRNA structure can influence protein expression levels.
  • The baculovirus/insect cell expression system is widely used for recombinant protein production.

Purpose of the Study:

  • To investigate the impact of synonymous mutations in signal peptide coding sequences on protein expression and secretion.
  • To determine the correlation between mRNA secondary structure, codon usage, and protein production.
  • To explore strategies for enhancing secretory protein production in insect cells.

Main Methods:

  • Introducing synonymous mutations into GP64sp and FibHsp signal peptide coding sequences.
  • Utilizing the baculovirus/insect cell expression system.
  • Analyzing mRNA secondary structure and codon bias.
  • Assessing protein production, secretion, and degradation levels (e.g., using MG-132).

Main Results:

  • mRNA structural stability of signal sequences did not correlate with protein production or secretion.
  • FibHsp tolerated codon changes better than GP64sp.
  • Increased codon usage frequency in GP64sp signal peptides led to reduced luciferase activity and secretion, and increased protein degradation, suggesting misfolding.
  • Introducing non-optimal codons into FibHsp signal peptides enhanced luciferase production and secretion.

Conclusions:

  • Synonymous codon substitutions in signal peptides can negatively impact protein production and secretion through misfolding.
  • Optimizing codon usage in signal peptides, specifically by incorporating non-optimal codons in certain sequences like FibHsp, can serve as a novel strategy to improve secretory protein yields in insect cells.