pH-dependent conformational changes of a Thogoto virus matrix protein reveal mechanisms of viral assembly and

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Mingrui Yang1,2, Feng Feng2, Yingfang Liu1,2

  • 1State Key Laboratory of Virology/Institute of Medical Virology, School of Basic Medical Sciences, Wuhan University, Wuhan 430071, PR China.

The Journal of General Virology
|July 15, 2016
PubMed

Insights

The matrix proteins of Thogoto virus undergo pH-dependent structural changes, revealing insights into viral capsid assembly and disassembly mechanisms for orthomyxoviruses.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Orthomyxoviruses, including influenza virus, are ssRNA viruses with essential matrix proteins.
  • The precise mechanisms of orthomyxovirus matrix proteins in viral life cycles are not fully understood.
  • Previous studies primarily focused on influenza virus matrix protein structure and function.

Purpose of the Study:

  • To elucidate the structural mechanisms of Thogoto virus matrix protein.
  • To investigate pH-dependent conformational changes in the N-terminal domain of Thogoto virus matrix protein.

Main Methods:

  • X-ray crystallography was used to determine the structure of the Thogoto virus matrix protein's N-terminal domain.
  • Structural analysis was performed at two different pH conditions (7.0 and 4.5).

Main Results:

  • The crystal structures of the Thogoto virus matrix protein N-terminal domain at pH 7.0 and 4.5 were determined.
  • Conformational changes in both monomeric and dimeric forms of the protein were observed across different pH levels.
  • These structural alterations are primarily attributed to the flexibility of the L3 and L5 loops.

Conclusions:

  • The identified pH-induced structural changes in Thogoto virus matrix protein provide a basis for understanding viral capsid assembly and disassembly.
  • This study expands the structural knowledge of orthomyxovirus matrix proteins beyond influenza virus.

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