Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins

Elsevier 2020-08-20

Lyssavirus P protein is a multifunctional protein that interacts with numerous host-cell proteins. The C-terminal domain (CTD) of P is important for inhibition of JAK-STAT signaling enabling the virus to evade host immunity. Several regions on the surface of rabies virus P are reported to interact with host factors. Among them, an extended, discrete hydrophobic patch of P CTD is notable. Although structures of P CTD of two strains of rabies virus, and of mokola virus have been solved, the structure of P CTD for Duvenhage virus, which is functionally divergent from these species for immune evasion function, is not known. Here, we analyze the structures of P CTD of Duvenhage and of a distinct rabies virus strain to gain further insight on the nature and potential function of the hydrophobic surface. Molecular contacts in crystals suggest that the hydrophobic patch is important to intermolecular interactions with other proteins, which differ between the lyssavirus species. (C) 2020 Elsevier Inc. All rights reserved.

Lyssavirus; P protein; Immune evasion; JAK-STAT pathway; Hydrophobic interaction; 464; Journal Article; AM

application/pdf
application/pdf
English

JPNII oai:irdb.nii.ac.jp:01364:0004998805
0006-291X
Biochemical and biophysical research communications, 529(2), 507-512
1375198965

NATIONAL INST OF INFO
From OAIster®, provided by the OCLC Cooperative.

edsoai.on1375198965