Abstract

Haemagglutinin and neuraminidase surface glycoproteins of the bat influenza H17N10 virus neither bind to nor cleave sialic acid receptors, indicating that this virus employs cell entry mechanisms distinct from those of classical influenza A viruses. We observed that certain human haematopoietic cancer cell lines and canine MDCK II cells are susceptible to H17-pseudotyped viruses. We identified the human HLA-DR receptor as an entry mediator for H17 pseudotypes, suggesting that H17N10 possesses zoonotic potential.

Highlights

  • The HA mediates virus binding to host-specific sialic acid (SA) moieties[4]

  • We have shown that transduction-competent H17- and H17N10-PV are recovered from HEK293T/17 cells only in the presence of proteases (HAT or TMPRSS2) (Fig. 1a)[13], in keeping with published data[11]

  • N10 transduced these cells with high, comparable efficiency, indicating that N10 is dispensable for entry, in keeping with published data[9,11]

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Summary

Introduction

To study the distribution of the H17N10 receptor(s), a panel of cell lines (Supplementary Table 1) was challenged with H17–PV, assaying transduction via the expression of PV-encoded luciferase reporter. MDCK II cells were not susceptible to PV expressing N10 alone while particles bearing H17 alone or both H17 and Entry of H17-PV was more affected than H5-PV by pre-treatment of cells with proteases or an inhibitor of N-glycosylation (reduced by up to 72 and 78%, compared to 45 and 20%, respectively), supporting the supposition[9] that the H17-receptor(s) is a glycoprotein. Using transmembrane domain and subcellular localisation prediction algorithms, we identified the dog leukocyte antigen DRαchain (DLA-DRA) as the only transcript encoding a surface-anchored protein, over-expressed in late, compared to early, passage cells (Supplementary Table 2).

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