scholarly journals Modulation of cell surface transport and lipid raft localization by the cytoplasmic tail of the influenza virus hemagglutinin

2015 ◽  
Vol 18 (1) ◽  
pp. 125-136 ◽  
Author(s):  
Silvia Scolari ◽  
Katharina Imkeller ◽  
Fabian Jolmes ◽  
Michael Veit ◽  
Andreas Herrmann ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Cell Surface ◽  
Lipid Raft ◽  
Cytoplasmic Tail ◽  
Surface Transport ◽  
Influenza Virus Hemagglutinin

scholarly journals Addition of truncated oligosaccharides to influenza virus hemagglutinin results in its temperature-conditional cell-surface expression.

1989 ◽  
Vol 108 (2) ◽  
pp. 355-365 ◽  
Author(s):  
J Hearing ◽  
M J Gething ◽  
J Sambrook
Keyword(s):  
Influenza Virus ◽  
Cell Surface ◽  
Cell Lines ◽  
Mutant Cell ◽  
Surface Expression ◽  
Ovary Cell ◽  
Cell Surface Expression ◽  
Permissive Temperature ◽  
Influenza Virus Hemagglutinin ◽  
Conditional Expression

In the preceding paper (Hearing, J., E. Hunter, L. Rodgers, M.-J. Gething, and J. Sambrook. 1989. J. Cell Biol. 108:339-353) we described the isolation and initial characterization of seven Chinese hamster ovary cell lines that are temperature conditional for the cell-surface expression of influenza virus hemagglutinin (HA) and other integral membrane glycoproteins. Two of these cell lines appeared to be defective for the synthesis and/or addition of mannose-rich oligosaccharide chains to nascent glycoproteins. In this paper we show that at both 32 and 39 degrees C in two mutant cell lines accumulate a truncated version, Man5GlcNAc2, of the normal lipid-linked precursor oligosaccharide, Glc3Man9GlcNAc2. This is possibly due to a defect in the synthesis of dolichol phosphate because in vitro assays indicate that the mutant cells are not deficient in mannosylphosphoryldolichol synthase at either temperature. A mixture of truncated and complete oligosaccharide chains was transferred to newly synthesized glycoproteins at both the permissive and restrictive temperatures. Both mutant cell lines exhibited altered sensitivity to cytotoxic plant lectins when grown at 32 degrees C, indicating that cellular glycoproteins bearing abnormal oligosaccharide chains were transported to the cell surface at the permissive temperature. Although glycosylation was defective at both 32 and 39 degrees C, the cell lines were temperature conditional for growth, suggesting that cellular glycoproteins were adversely affected by the glycosylation defect at the elevated temperature. The temperature-conditional expression of HA on the cell surface was shown to be due to impairment at 39 degrees C of the folding, trimerization, and stability of HA molecules containing truncated oligosaccharide chains.

scholarly journals The Role of the Cytoplasmic Tail Region of Influenza Virus Hemagglutinin in Formation and Growth of Fusion Pores

Virology ◽  
1997 ◽  
Vol 235 (1) ◽  
pp. 118-128 ◽  
Author(s):  
Grigory B. Melikyan ◽  
Hong Jin ◽  
Robert A. Lamb ◽  
Fredric S. Cohen
Keyword(s):  
Influenza Virus ◽  
Cytoplasmic Tail ◽  
Tail Region ◽  
Influenza Virus Hemagglutinin ◽  
Fusion Pores

scholarly journals Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin.

1991 ◽  
Vol 65 (5) ◽  
pp. 2491-2500 ◽  
Author(s):  
M Veit ◽  
E Kretzschmar ◽  
K Kuroda ◽  
W Garten ◽  
M F Schmidt ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Cytoplasmic Tail ◽  
Cysteine Residues ◽  
Site Specific ◽  
Influenza Virus Hemagglutinin

scholarly journals Fusion Activity of Transmembrane and Cytoplasmic Domain Chimeras of the Influenza Virus Glycoprotein Hemagglutinin

1998 ◽  
Vol 72 (1) ◽  
pp. 133-141 ◽  
Author(s):  
Britta Schroth-Diez ◽  
Evgeni Ponimaskin ◽  
Helmut Reverey ◽  
Michael F. G. Schmidt ◽  
Andreas Herrmann
Keyword(s):  
Influenza Virus ◽  
Membrane Fusion ◽  
Lipid Bilayers ◽  
Transmembrane Domain ◽  
Sendai Virus ◽  
Expression System ◽  
Cytoplasmic Tail ◽  
Fusion Pore ◽  
Fusion Activity ◽  
Influenza Virus Hemagglutinin

ABSTRACT The role of the sequence of transmembrane and cytoplasmic/intraviral domains of influenza virus hemagglutinin (HA, subtype H7) for HA-mediated membrane fusion was explored. To analyze the influence of the two domains on the fusogenic properties of HA, we designed HA-chimeras in which the cytoplasmic tail and/or transmembrane domain of HA was replaced with the corresponding domains of the fusogenic glycoprotein F of Sendai virus. These chimeras, as well as constructs of HA in which the cytoplasmic tail was replaced by peptides of human neurofibromin type1 (NF1) or c-Raf-1, NF78 (residues 1441 to 1518), and Raf81 (residues 51 to 131), respectively, were expressed in CV-1 cells by using the vaccinia virus-T7 polymerase transient-expression system. Wild-type and chimeric HA were cleaved properly into two subunits and expressed as trimers. Membrane fusion between CV-1 cells and bound human erythrocytes (RBCs) mediated by parental or chimeric HA proteins was studied by a lipid-mixing assay with the lipid-like fluorophore octadecyl rhodamine B chloride (R18). No profound differences in either extent or kinetics could be observed. After the pH was lowered, the above proteins also induced a flow of the aqueous fluorophore calcein from preloaded RBCs into the cytoplasm of the protein-expressing CV-1 cells, indicating that membrane fusion involves both leaflets of the lipid bilayers and leads to formation of an aqueous fusion pore. We conclude that neither HA-specific sequences in the transmembrane and cytoplasmic domains nor their length is crucial for HA-induced membrane fusion activity.

scholarly journals Cholesterol Is Required for Surface Transport of Influenza Virus Hemagglutinin

1998 ◽  
Vol 140 (6) ◽  
pp. 1357-1367 ◽  
Author(s):  
Patrick Keller ◽  
Kai Simons
Keyword(s):  
Influenza Virus ◽  
Membrane Proteins ◽  
Basolateral Membrane ◽  
Surface Transport ◽  
Influenza Virus Hemagglutinin ◽  
Vesicular Stomatitis ◽  
Apical Sorting ◽  
Triton X ◽  
Level Of Living ◽  
First Time

Transport from the TGN to the basolateral surface involves a rab/N-ethylmaleimide–sensitive fusion protein (NSF)/soluble NSF attachment protein (SNAP)/SNAP receptor (SNARE) mechanism. Apical transport instead is thought to be mediated by detergent-insoluble sphingolipid–cholesterol rafts. By reducing the cholesterol level of living cells by 60–70% with lovastatin and methyl-β-cyclodextrin, we show that the TGN-to-surface transport of the apical marker protein influenza virus hemagglutinin was slowed down, whereas the transport of the basolateral marker vesicular stomatitis virus glycoprotein as well as the ER-to-Golgi transport of both membrane proteins was not affected. Reduction of transport of hemagglutinin was accompanied by increased solubility in the detergent Triton X-100 and by significant missorting of hemagglutinin to the basolateral membrane. In addition, depletion of cellular cholesterol by lovastatin and methyl-β-cyclodextrin led to missorting of the apical secretory glycoprotein gp-80, suggesting that gp-80 uses a raft-dependent mechanism for apical sorting. Our data provide for the first time direct evidence for the functional significance of cholesterol in the sorting of apical membrane proteins as well as of apically secreted glycoproteins.

Sign in / Sign up

Export Citation Format

Share Document