Mobilization and aggregation of integral membrane proteins in erythrocytes induced by interaction with influenza virus at acidic pH

Akihiko Yoshimura, Shohei Yamashina, Shun Ichi Ohnishi

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Effect of influenza virus on erythrocyte membranes was investigated by electron microscopy and fluorescence photobleaching recovery measurements. The virus induced mobilization of integral proteins in erythrocyte membrane at acidic pH, where it fused with the cell membrane to cause hemolysis and also cell fusions but not at neutral pH. At lower temperatures (e.g., 4 °C), the proteins aggregated in the membrane and, consequently, large protein-free lipid bilayer area was produced. At higher temperatures (e.g., 37 °C) the protein distribution became randomized. Spectrin meshwork underneath the erythrocyte membrane was also markedly modified by the virus at acidic pH. Diffuse fibril structure was converted into dense spots and the membrane area lacking the fibril structure was produced. Isolated hemagglutinin rosettes also caused mobilization and aggregation of the integral proteins at acidic pH but to smaller extent than that induced by virus. The membrane perturbation detected as the protein mobilization by the action of hemagglutinin was assigned to be the cause for envelope fusion.

Original languageEnglish
Pages (from-to)126-137
Number of pages12
JournalExperimental Cell Research
Volume160
Issue number1
DOIs
Publication statusPublished - 1985
Externally publishedYes

Fingerprint

Orthomyxoviridae
Membrane Proteins
Erythrocyte Membrane
Erythrocytes
Hemagglutinins
Protein C
Viruses
Membranes
Proteins
Fluorescence Recovery After Photobleaching
Spectrin
Temperature
Cell Fusion
Lipid Bilayers
Hemolysis
Electron Microscopy
Cell Membrane

ASJC Scopus subject areas

  • Cell Biology

Cite this

Mobilization and aggregation of integral membrane proteins in erythrocytes induced by interaction with influenza virus at acidic pH. / Yoshimura, Akihiko; Yamashina, Shohei; Ohnishi, Shun Ichi.

In: Experimental Cell Research, Vol. 160, No. 1, 1985, p. 126-137.

Research output: Contribution to journalArticle

@article{b050920fe2834077b85875aa70213d73,
title = "Mobilization and aggregation of integral membrane proteins in erythrocytes induced by interaction with influenza virus at acidic pH",
abstract = "Effect of influenza virus on erythrocyte membranes was investigated by electron microscopy and fluorescence photobleaching recovery measurements. The virus induced mobilization of integral proteins in erythrocyte membrane at acidic pH, where it fused with the cell membrane to cause hemolysis and also cell fusions but not at neutral pH. At lower temperatures (e.g., 4 °C), the proteins aggregated in the membrane and, consequently, large protein-free lipid bilayer area was produced. At higher temperatures (e.g., 37 °C) the protein distribution became randomized. Spectrin meshwork underneath the erythrocyte membrane was also markedly modified by the virus at acidic pH. Diffuse fibril structure was converted into dense spots and the membrane area lacking the fibril structure was produced. Isolated hemagglutinin rosettes also caused mobilization and aggregation of the integral proteins at acidic pH but to smaller extent than that induced by virus. The membrane perturbation detected as the protein mobilization by the action of hemagglutinin was assigned to be the cause for envelope fusion.",
author = "Akihiko Yoshimura and Shohei Yamashina and Ohnishi, {Shun Ichi}",
year = "1985",
doi = "10.1016/0014-4827(85)90242-3",
language = "English",
volume = "160",
pages = "126--137",
journal = "Experimental Cell Research",
issn = "0014-4827",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Mobilization and aggregation of integral membrane proteins in erythrocytes induced by interaction with influenza virus at acidic pH

AU - Yoshimura, Akihiko

AU - Yamashina, Shohei

AU - Ohnishi, Shun Ichi

PY - 1985

Y1 - 1985

N2 - Effect of influenza virus on erythrocyte membranes was investigated by electron microscopy and fluorescence photobleaching recovery measurements. The virus induced mobilization of integral proteins in erythrocyte membrane at acidic pH, where it fused with the cell membrane to cause hemolysis and also cell fusions but not at neutral pH. At lower temperatures (e.g., 4 °C), the proteins aggregated in the membrane and, consequently, large protein-free lipid bilayer area was produced. At higher temperatures (e.g., 37 °C) the protein distribution became randomized. Spectrin meshwork underneath the erythrocyte membrane was also markedly modified by the virus at acidic pH. Diffuse fibril structure was converted into dense spots and the membrane area lacking the fibril structure was produced. Isolated hemagglutinin rosettes also caused mobilization and aggregation of the integral proteins at acidic pH but to smaller extent than that induced by virus. The membrane perturbation detected as the protein mobilization by the action of hemagglutinin was assigned to be the cause for envelope fusion.

AB - Effect of influenza virus on erythrocyte membranes was investigated by electron microscopy and fluorescence photobleaching recovery measurements. The virus induced mobilization of integral proteins in erythrocyte membrane at acidic pH, where it fused with the cell membrane to cause hemolysis and also cell fusions but not at neutral pH. At lower temperatures (e.g., 4 °C), the proteins aggregated in the membrane and, consequently, large protein-free lipid bilayer area was produced. At higher temperatures (e.g., 37 °C) the protein distribution became randomized. Spectrin meshwork underneath the erythrocyte membrane was also markedly modified by the virus at acidic pH. Diffuse fibril structure was converted into dense spots and the membrane area lacking the fibril structure was produced. Isolated hemagglutinin rosettes also caused mobilization and aggregation of the integral proteins at acidic pH but to smaller extent than that induced by virus. The membrane perturbation detected as the protein mobilization by the action of hemagglutinin was assigned to be the cause for envelope fusion.

UR - http://www.scopus.com/inward/record.url?scp=0022356596&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022356596&partnerID=8YFLogxK

U2 - 10.1016/0014-4827(85)90242-3

DO - 10.1016/0014-4827(85)90242-3

M3 - Article

VL - 160

SP - 126

EP - 137

JO - Experimental Cell Research

JF - Experimental Cell Research

SN - 0014-4827

IS - 1

ER -