Author: Hoffmann, Markus; González Hernández, Mariana; Berger, Elisabeth; Marzi, Andrea; Pöhlmann, Stefan
Title: The Glycoproteins of All Filovirus Species Use the Same Host Factors for Entry into Bat and Human Cells but Entry Efficiency Is Species Dependent Document date: 2016_2_22
ID: 146cwh6y_32
Snippet: A MLD and a furin-cleavage site are present in all filovirus GPs. Nevertheless, these elements are dispensable for entry into human cells lines and, in case of the furin cleavage site, for viral spread and pathogenesis in the host [23, 24, [57] [58] [59] [60] . A scenario accounting for these discrepant findings could be that these elements are required for entry into reservoir but not NHP and human cells. The present study shows that this is not.....
Document: A MLD and a furin-cleavage site are present in all filovirus GPs. Nevertheless, these elements are dispensable for entry into human cells lines and, in case of the furin cleavage site, for viral spread and pathogenesis in the host [23, 24, [57] [58] [59] [60] . A scenario accounting for these discrepant findings could be that these elements are required for entry into reservoir but not NHP and human cells. The present study shows that this is not the case, since neither inactivation of the cleavage site nor deletion of the MLD appreciably altered transduction of the fruit bat cell lines investigated. One could speculate that the MLD is required for efficient spread in the host, potentially by modulating immune recognition of GP, and is thus present in all filovirus GPs. Why the GP motif for processing by furin or other proprotein convertases is conserved requires further investigation.
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