Lipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein Erns
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چکیده
منابع مشابه
Lipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein Erns
Pestiviruses express a peculiar protein named Erns representing envelope glycoprotein and RNase, which is important for control of the innate immune response and persistent infection. The latter functions are connected with secretion of a certain amount of Erns from the infected cell. Retention/secretion of Erns is most likely controlled by its unusual membrane anchor, a long amphipathic helix ...
متن کاملStructure of the Membrane Anchor of Pestivirus Glycoprotein Erns, a Long Tilted Amphipathic Helix
E(rns) is an essential virion glycoprotein with RNase activity that suppresses host cellular innate immune responses upon being partially secreted from the infected cells. Its unusual C-terminus plays multiple roles, as the amphiphilic helix acts as a membrane anchor, as a signal peptidase cleavage site, and as a retention/secretion signal. We analyzed the structure and membrane binding propert...
متن کاملThe pestivirus glycoprotein Erns is anchored in plane in the membrane via an amphipathic helix.
E(rns) is a structural glycoprotein of pestiviruses found to be attached to the virion and to membranes within infected cells via its COOH terminus, although it lacks a hydrophobic anchor sequence. The COOH-terminal sequence was hypothesized to fold into an amphipathic alpha-helix. Alanine insertion scanning revealed that the ability of the E(rns) COOH terminus to bind membranes is considerably...
متن کاملThe Pestivirus Glycoprotein E Is Anchored in Plane in the Membrane via an Amphipathic Helix*
Erns is a structural glycoprotein of pestiviruses found to be attached to the virion and tomembraneswithin infected cells via its COOH terminus, although it lacks a hydrophobic anchor sequence. The COOH-terminal sequence was hypothesized to fold into an amphipathic -helix. Alanine insertion scanning revealed that the ability of the Erns COOH terminus to bind membranes is considerably reduced by...
متن کاملLipid binding to the amphipathic membrane protein cytochrome b5.
The lipid binding properties of the membrane protein cytochrome b(5) (detergent-extracted from calf liver microsomal preparations) were characterized by studying the interaction of spin-labeled lipids (5-, 12-, and 16-doxylstearic acid and 5- and 16-doxylphosphatidyl-choline, where doxyl refers to the nitroxide moiety) with cytochrome b(5), using electron spin resonance spectroscopy. The intact...
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ژورنال
عنوان ژورنال: PLOS ONE
سال: 2015
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0135680