Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide make significant contributions to fusion of membrane vesicles
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- 作者：Punsisi U. Ratnayake ; E.A. Prabodha Ekanayaka ; Sweta S. Komanduru ; David P. Weliky ; weliky@chemistry.msu.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Buffer A ; 50 ; mM phosphate ; 0.5% SRC ; 50 ; mM sodium phosphate ; and 300 ; mM NaCl at pH 8.0 ; Buffer B ; 10 ; mM Tris&ndash ; HCl ; 0.17% DM ; and 1 ; mM DTT at pH 7.4 ; Buffer C ; 10 ; mM Tris&ndash ; HCl ; 0.10% SRC ; and 1 ; mM DTT at pH 7.4 ; CD ; circular dichroism ; DM ; decylmaltoside ; DOTAP ; 1 ; 2-dioleoyl-3-trimethylammonium-propane (chloride salt) ; DTT ; dithiothreitol ; Endo ; endodomain ; FP ; fusion peptide ; HA ; hemagglutinin ; HA-cell ; HA-expressing cell ; HEPES ; 4-(2-hydroxyethyl)-1-
- 刊名：Protein Expression and Purification
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：117
- 期：Complete
- 页码：6-16
- 全文大小：1563 K
文摘
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Milligram quantities of full-length influenza virus hemagglutinin II protein.
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Hyperthermostable folded HA2 trimers at pH 7.4.
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Extensive HA2-catalyzed fusion of negatively-charged vesicles at pH 5.0.
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Extensive HA2-catalyzed fusion of positively-charged vesicles at pH 7.4.
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Significant contributions to fusion from the soluble ectodomain and fusion peptide.