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Mutations in the FPIV motif of Newcastle disease virus matrix protein attenuate virus replication and reduce virus

Zhiqiang Duan1, Zenglei Hu, Jie Zhu

  • 1Animal Infectious Disease Laboratory, College of Veterinary Medicine, Yangzhou University, 12 East Wenhui Road, Yangzhou, 225009, Jiangsu, China.

Archives of Virology
|January 31, 2014
PubMed

Insights

The Newcastle disease virus (NDV) matrix protein contains a critical FPIV motif essential for viral replication and budding. This motif, particularly phenylalanine and proline residues, is vital for virus release, potentially involving cellular multivesicular body pathways.

Area of Science:

  • Virology
  • Molecular Biology

Background:

  • Late domains in matrix proteins of certain viruses are crucial for viral budding.
  • The FPIV sequence motif was previously identified in parainfluenza virus 5 and mumps virus.

Purpose of the Study:

  • To investigate the presence and role of the FPIV motif in the Newcastle disease virus (NDV) matrix (M) protein.
  • To elucidate the mechanism of NDV replication and budding.

Main Methods:

  • Sequence analysis to identify the FPIV motif in NDV M protein.
  • Site-directed mutagenesis to alter phenylalanine (F) and proline (P) residues.
  • Viral replication and budding assays.
  • Expression of dominant-negative VPS4A-E228Q to assess involvement of the multivesicular body pathway.

Main Results:

  • The FPIV sequence motif was identified at the N-terminus of the NDV M protein.
  • Mutations in F or P residues significantly reduced viral virulence, replication, and budding.
  • Inhibition of NDV production was observed upon expression of dominant-negative VPS4A-E228Q, suggesting MVB pathway involvement.

Conclusions:

  • The FPIV motif, particularly F and P residues, is critical for NDV M protein function in replication and budding.
  • NDV budding likely utilizes the cellular multivesicular body (MVB) pathway.

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