Skip to main content

The Influenza Virus Neuraminidase Protein Trans-membrane and Head Domains Have Coevolved

da Silva, D, Nordholm, J, Dou, D, Wang, H, Rossman, Jeremy S., Daniels, R (2014) The Influenza Virus Neuraminidase Protein Trans-membrane and Head Domains Have Coevolved. Journal of Virology, 89 (2). pp. 1094-1104. ISSN 0022-538X. E-ISSN 1098-5514. (doi:10.1128/JVI.02005-14) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1128/JVI.02005-14

Abstract

Trans-membrane domains (TMDs) from single-spanning membrane proteins are commonly viewed as membrane anchors for functional domains. Influenza virus neuraminidase (NA) exemplifies this concept, as it retains enzymatic function upon proteolytic release from the membrane. However, the subtype 1 NA TMDs have become increasingly more polar in human strains since 1918, which suggests that selection pressure exists on this domain. Here, we investigated the N1 TMD-head domain relationship by exchanging a prototypical “old” TMD (1933) with a “recent” (2009), more polar TMD and an engineered hydrophobic TMD. Each exchange altered the TMD association, decreased the NA folding efficiency, and significantly reduced viral budding and replication at 37°C compared to at 33°C, at which NA folds more efficiently. Passaging the chimera viruses at 37°C restored the NA folding efficiency, viral budding, and infectivity by selecting for NA TMD mutations that correspond with their polar or hydrophobic assembly properties. These results demonstrate that single-spanning membrane protein TMDs can influence distal domain folding, as well as membrane-related processes, and suggest the NA TMD in H1N1 viruses has become more polar to maintain compatibility with the evolving enzymatic head domain.

Item Type: Article
DOI/Identification number: 10.1128/JVI.02005-14
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Jeremy Rossman
Date Deposited: 30 Oct 2014 11:02 UTC
Last Modified: 29 May 2019 13:18 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/43774 (The current URI for this page, for reference purposes)
  • Depositors only (login required):