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Updated: Dec 26, 2025

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
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Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit

Published on: June 28, 2013

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pH-dependent secondary structure propensity of the influenza A virus M2 cytoplasmic tail

Jolyon K Claridge1, Faiz Mohd-Kipli1, Andrei Florea1

  • 1Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.

Biomolecular NMR Assignments
|March 12, 2020
PubMed

Insights

The influenza A virus M2 protein's cytoplasmic tail, crucial for host interactions, shows mostly disordered structure. Key motifs exhibit specific conformations, aiding future research on viral and host factors.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • The matrix protein 2 (M2) C-terminal tail of influenza A virus is conserved and interacts with host proteins and M1.
  • High-resolution structural data for the M2 cytoplasmic tail is limited, unlike its transmembrane domain.

Purpose of the Study:

  • To characterize the structure of the M2 protein's cytoplasmic tail.
  • To investigate conformational changes under varying conditions like low pH and membrane mimetics.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine chemical shifts.
  • Chemical shift perturbations were analyzed at low pH and in the presence of membrane mimetics.

Main Results:

  • The M2 cytoplasmic tail is predominantly disordered.
  • The LC3 binding motif adopts an extended backbone conformation.
  • The M1 interaction site shows partial helical content with minor pH dependence.

Conclusions:

  • NMR chemical shift assignments provide a foundation for further studies.
  • Understanding M2 tail structure is key to elucidating its interactions with viral and host factors.
Keywords:
InfluenzaM2Matrix protein 2

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