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Cryptic epitopes and functional diversity in extracellular proteins.

Gysell M Mortimer1, Rodney F Minchin1

  • 1Laboratory for Molecular and Cellular Pharmacology, School of Biomedical Sciences, The University of Queensland, St. Lucia, Brisbane, Queensland, 4072, Australia.

The International Journal of Biochemistry & Cell Biology
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Protein unfolding and refolding expose hidden functional sequences, increasing protein diversity. This mechanism, particularly in extracellular proteins, offers new ways to regulate protein function.

Keywords:
Cryptic epitopesProtein conformationProtein unfolding

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein functional diversity is crucial for cellular and tissue complexity.
  • Translational and post-translational modifications are known sources of protein diversity.
  • Protein unfolding/refolding is an emerging mechanism for generating functional diversity by exposing cryptic sequences.

Purpose of the Study:

  • To review the role of protein unfolding and refolding in generating functional diversity.
  • To focus on extracellular proteins and the factors influencing their folding dynamics.
  • To explore the potential for manipulating protein function through understanding cryptic epitope exposure.

Main Methods:

  • Literature review focusing on extracellular protein dynamics.
  • Analysis of mechanisms influencing protein folding (mechanical forces, interactions, denaturation).
  • Examination of unfolding/refolding versus proteolytic cleavage in epitope exposure.

Main Results:

  • Extracellular protein folding dynamics are influenced by mechanical forces, protein-protein interactions, and denaturation.
  • While proteolytic cleavage exposes cryptic epitopes, unfolding/refolding is increasingly recognized for its role.
  • Unmasking of buried or cryptic sequences (epitopes) through unfolding/refolding imparts physiological functions.

Conclusions:

  • Protein unfolding and refolding represent a significant mechanism for increasing functional diversity, especially in extracellular proteins.
  • Understanding the dynamics of cryptic epitope exposure can lead to novel methods for protein function manipulation.
  • This review highlights the physiological relevance of folding dynamics in regulating extracellular protein behavior.