2yq2
From Proteopedia
Structure of BVDV1 envelope glycoprotein E2, pH8
Structural highlights
FunctionPOLG_BVDVS Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation.[UniProtKB:P19711] Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Also plays a role in transcription regulation. Protects the incoming virus against IFN-induced effectors.[UniProtKB:P19712] Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans (By similarity). Possesses also intrinsic ribonuclease (RNase) activity that can inhibit the production of type I interferon and assist in the development of persistent infections (By similarity).[UniProtKB:P19711][UniProtKB:Q96662] E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.[UniProtKB:P19711] E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (By similarity). Probably functions as a coeffector of fusion providing structural integrity to the fusion complex and possibly controlling exposure of the fusion motif in E1 (By similarity).[UniProtKB:P19711] Plays an essential role in the virus replication cycle by acting as a viroporin (By similarity). Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules (By similarity). Forms a leader sequence to properly orient NS2 in the membrane.[UniProtKB:P19712] Uncleaved NS2-3 is required for production of infectious virus. Plays a role in the regulation of viral RNA replication.[UniProtKB:P19712] Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity.[UniProtKB:P19712] Acts as a cofactor for the NS3 protease activity.[UniProtKB:P19712] Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). Plays a role in the inhibition of host innate immune response by inhibiting RIGI/IFIH1-mediated IFN-beta production (By similarity).[UniProtKB:P19711][UniProtKB:P19712] Replicates the viral (+) and (-) genome. Initiates the primer-independent RNA replication via a de novo mechanism requiring GTP (By similarity).[UniProtKB:P19711] Publication Abstract from PubMedEnveloped viruses have developed various adroit mechanisms to invade their host cells. This process requires one or more viral envelope glycoprotein to achieve cell attachment and membrane fusion. Members of the Flaviviridae such as flaviviruses possess only one envelope glycoprotein, E, whereas pestiviruses and hepacivirus encode two glycoproteins, E1 and E2. Although E2 is involved in cell attachment, it has been unclear which protein is responsible for membrane fusion. We report the crystal structures of the homodimeric glycoprotein E2 from the pestivirus bovine viral diarrhea virus 1 (BVDV1) at both neutral and low pH. Unexpectedly, BVDV1 E2 does not have a class II fusion protein fold, and at low pH the N-terminal domain is disordered, similarly to the intermediate postfusion state of E2 from sindbis virus, an alphavirus. Our results suggest that the pestivirus and possibly the hepacivirus fusion machinery are unlike any previously observed. Structure of a Pestivirus Envelope Glycoprotein E2 Clarifies Its Role in Cell Entry.,El Omari K, Iourin O, Harlos K, Grimes JM, Stuart DI Cell Rep. 2012 Dec 26. pii: S2211-1247(12)00424-X. doi:, 10.1016/j.celrep.2012.12.001. PMID:23273918[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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