Category: Proteins & Peptides

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Reference: CSB-BP365892HIL_100

Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP-independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral pol, host NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the whole ssDNA genome during synthesis. The complementary strand synthesis induces its relese from DNA template. May inhibit cellular transcription mediated by the interaction between host SRCAP and CBP.

Reference: CSB-BP365892HIL_20

Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP-independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral pol, host NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the whole ssDNA genome during synthesis. The complementary strand synthesis induces its relese from DNA template. May inhibit cellular transcription mediated by the interaction between host SRCAP and CBP.

Reference: CSB-BP365937HPO_500

Attaches the virion to the host cell mbrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hagglutinating activities.Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors.

Reference: CSB-BP365937HPO_100

Attaches the virion to the host cell mbrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hagglutinating activities.Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors.

Reference: CSB-BP365937HPO_20

Attaches the virion to the host cell mbrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hagglutinating activities.Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors.

Reference: CSB-BP365970RID_100

Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane. There is convincing in vitro evidence that the muscular form of the nicotinic acetylcholine receptor, the neuronal cell adhesion molecule, and the p75 neurotrophin receptor bind glycoprotein and thereby facilitate rabies virus entry into cells.

Reference: CSB-BP365970RID_20

Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane. There is convincing in vitro evidence that the muscular form of the nicotinic acetylcholine receptor, the neuronal cell adhesion molecule, and the p75 neurotrophin receptor bind glycoprotein and thereby facilitate rabies virus entry into cells.

Reference: CSB-BP365972RIX_1

Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP.