Abstract:
:Cell entry of many enveloped viruses occurs by engagement with cellular receptors, followed by internalization into endocytic compartments and pH-induced membrane fusion. A previously unnoticed step of receptor switching was found to be critical during cell entry of two devastating human pathogens: Ebola and Lassa viruses. Our recent studies revealed the functional role of receptor switching to LAMP1 for triggering membrane fusion by Lassa virus and showed the involvement of conserved histidines in this switching, suggesting that other viruses from this family may also switch to LAMP1. However, when we investigated viruses that are genetically close to Lassa virus, we discovered that they cannot bind LAMP1. A crystal structure of the receptor-binding module from Morogoro virus revealed structural differences that allowed mapping of the LAMP1 binding site to a unique set of Lassa residues not shared by other viruses in its family, illustrating a key difference in the cell-entry mechanism of Lassa virus that may contribute to its pathogenicity.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Israeli H,Cohen-Dvashi H,Shulman A,Shimon A,Diskin Rdoi
10.1371/journal.ppat.1006337subject
Has Abstractpub_date
2017-04-27 00:00:00pages
e1006337issue
4eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-17-00183journal_volume
13pub_type
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