Author: Hunt, Catherine L.; Lennemann, Nicholas J.; Maury, Wendy
Title: Filovirus Entry: A Novelty in the Viral Fusion World Document date: 2012_2_7
ID: 1j9zmuub_16
Snippet: C-type lectin family members L-SIGN, DC-SIGN and hMGL have been shown to enhance filovirus entry [19, [44] [45] [46] [47] [48] . Studies have demonstrated that both the mucin domain and the glycan cap of GP 1 interact with C-type lectins [47, 49] . However, as both of these regions can be deleted from EBOV GP 1 without loss of viral transduction efficiency [16, [50] [51] [52] , it is likely that C-type lectins increase filovirus attachment to cel.....
Document: C-type lectin family members L-SIGN, DC-SIGN and hMGL have been shown to enhance filovirus entry [19, [44] [45] [46] [47] [48] . Studies have demonstrated that both the mucin domain and the glycan cap of GP 1 interact with C-type lectins [47, 49] . However, as both of these regions can be deleted from EBOV GP 1 without loss of viral transduction efficiency [16, [50] [51] [52] , it is likely that C-type lectins increase filovirus attachment to cells rather than serving as cellular receptors that mediate internalization of the virus into endosomes [53] . A similar adherence function for C-type lectins has been identified for other enveloped viruses such as HIV [54] .
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