Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 529, Issue 2, Pages 507-512Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2020.05.195
Keywords
Lyssavirus; P protein; Immune evasion; JAK-STAT pathway; Hydrophobic interaction
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Funding
- Japan Society for the Promotion of Science KAKENHI [17K07296]
- National Health and Medical Research Council Australia [1125704]
- Platform Project for Supporting Drug Discovery and Life Science Research - Japan AMED
- Hokkaido University
- Global Facility Center and Pharma Science Open Unit - MEXT under Support Program for Implementation of New Equipment Sharing System
- Grants-in-Aid for Scientific Research [17K07296] Funding Source: KAKEN
- National Health and Medical Research Council of Australia [1125704] Funding Source: NHMRC
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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.
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