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Proteolytic processing of Middle East respiratory syndrome coronavirus spikes expands virus tropism
Journal article   Open access   Peer reviewed

Proteolytic processing of Middle East respiratory syndrome coronavirus spikes expands virus tropism

Jung-Eun Park, Kun Li, Arlene Barlan, Anthony R Fehr, Stanley Perlman, Paul B McCray Jr and Tom Gallagher
Proceedings of the National Academy of Sciences, USA, Vol.113(43), pp.12262-12262
10/01/2016
DOI: 10.1073/pnas.1608147113
PMCID: PMC5086990
PMID: 27791014
url
https://europepmc.org/articles/pmc5086990View
Published (Version of record) Open Access

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) infects humans from zoonotic sources and causes severe pulmonary disease. Virions require spike (S) glycoproteins for binding to cell receptors and for catalyzing virus-cell membrane fusion. Fusion occurs only after S proteins are cleaved sequentially, first during their secretion through the exocytic organelles of virus-producing cells, and second after virus binding to target-cell receptors. To more precisely determine how sequential proteolysis contributes to CoV infection, we introduced S mutations obstructing the first cleavages. These mutations severely compromised MERS-CoV infection into human lung-derived cells, but had little effect on infection into several other cell types. These cell type-specific requirements for proteolysis correlated with S conformations during cell entry. Without the first cleavages, S proteins resisted cell receptor-induced conformational changes, which restricted the second, fusion-activating cleavages. Consistent with these findings, precleaved MERS viruses used receptor-proximal, cell-surface proteases to effect the second fusion-activating cleavages during cell entry, whereas the more rigid uncleaved MERS viruses trafficked past these cell-surface proteases and into endosomes. Uncleaved viruses were less infectious to human airway epithelial and Calu3 cell cultures because they lacked sufficient endosomal fusion-activating proteases. Thus, by sensitizing viruses to receptor-induced conformational changes, the first S cleavages expand virus tropism to cell types that are relevant to lung infection, and therefore may be significant determinants of MERS-CoV virulence.

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