The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin

Janette Lazarovits, Shang Pwu Shia, Nicholas Ktistakis, Myeong Sok Lee, Catharina Bird, Michael G. Roth

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Eleven chimeric proteins were created in which the transmembrane, the cytoplasmic, or both topological domains of the influenza virus hemagglutinin (HA) were replaced with those from five other glycoproteins. All of the chimeric HAs reached the cell surface but appeared to differ in the degree to which they were stably folded. Comparisons of the rates of folding, passage into the Golgi, and arrival at the plasma membrane of wild-type HA and the chimeric proteins suggest that formation of a stable HA trimer is not an absolute requirement for export from the endoplasmic reticulum. In addition, there appear to be at least two steps at which the rate of transport can be altered during exocytosis, one occurring before and the other after the trimming of oligosaccharides by Golgi mannosidases. Certain of the chimeras differed from HA in their ability to pass through each of these steps. Replacement of the HA transmembrane domain with the analogous sequences from other proteins affected folding and transport of the chimeric HAs in ways that suggest that the HA transmembrane sequences form a specific structure in the membrane that differs from that formed by analogous sequences from the other proteins.

Original languageEnglish (US)
Pages (from-to)4760-4767
Number of pages8
JournalJournal of Biological Chemistry
Volume265
Issue number8
StatePublished - Mar 15 1990

Fingerprint

Biosynthesis
Hemagglutinins
Orthomyxoviridae
Viruses
Proteins
Mannosidases
Trimming
Protein Folding
Exocytosis
Protein Transport
Cell membranes
Oligosaccharides
Endoplasmic Reticulum
Glycoproteins
Cell Membrane
Membranes

ASJC Scopus subject areas

  • Biochemistry

Cite this

The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin. / Lazarovits, Janette; Shia, Shang Pwu; Ktistakis, Nicholas; Lee, Myeong Sok; Bird, Catharina; Roth, Michael G.

In: Journal of Biological Chemistry, Vol. 265, No. 8, 15.03.1990, p. 4760-4767.

Research output: Contribution to journalArticle

Lazarovits, J, Shia, SP, Ktistakis, N, Lee, MS, Bird, C & Roth, MG 1990, 'The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin', Journal of Biological Chemistry, vol. 265, no. 8, pp. 4760-4767.
Lazarovits, Janette ; Shia, Shang Pwu ; Ktistakis, Nicholas ; Lee, Myeong Sok ; Bird, Catharina ; Roth, Michael G. / The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 8. pp. 4760-4767.
@article{9c44b4b6ddd345bd82328adcb295c4e3,
title = "The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin",
abstract = "Eleven chimeric proteins were created in which the transmembrane, the cytoplasmic, or both topological domains of the influenza virus hemagglutinin (HA) were replaced with those from five other glycoproteins. All of the chimeric HAs reached the cell surface but appeared to differ in the degree to which they were stably folded. Comparisons of the rates of folding, passage into the Golgi, and arrival at the plasma membrane of wild-type HA and the chimeric proteins suggest that formation of a stable HA trimer is not an absolute requirement for export from the endoplasmic reticulum. In addition, there appear to be at least two steps at which the rate of transport can be altered during exocytosis, one occurring before and the other after the trimming of oligosaccharides by Golgi mannosidases. Certain of the chimeras differed from HA in their ability to pass through each of these steps. Replacement of the HA transmembrane domain with the analogous sequences from other proteins affected folding and transport of the chimeric HAs in ways that suggest that the HA transmembrane sequences form a specific structure in the membrane that differs from that formed by analogous sequences from the other proteins.",
author = "Janette Lazarovits and Shia, {Shang Pwu} and Nicholas Ktistakis and Lee, {Myeong Sok} and Catharina Bird and Roth, {Michael G.}",
year = "1990",
month = "3",
day = "15",
language = "English (US)",
volume = "265",
pages = "4760--4767",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "8",

}

TY - JOUR

T1 - The effects of foreign transmembrane domains on the biosynthesis of the influenza virus hemagglutinin

AU - Lazarovits, Janette

AU - Shia, Shang Pwu

AU - Ktistakis, Nicholas

AU - Lee, Myeong Sok

AU - Bird, Catharina

AU - Roth, Michael G.

PY - 1990/3/15

Y1 - 1990/3/15

N2 - Eleven chimeric proteins were created in which the transmembrane, the cytoplasmic, or both topological domains of the influenza virus hemagglutinin (HA) were replaced with those from five other glycoproteins. All of the chimeric HAs reached the cell surface but appeared to differ in the degree to which they were stably folded. Comparisons of the rates of folding, passage into the Golgi, and arrival at the plasma membrane of wild-type HA and the chimeric proteins suggest that formation of a stable HA trimer is not an absolute requirement for export from the endoplasmic reticulum. In addition, there appear to be at least two steps at which the rate of transport can be altered during exocytosis, one occurring before and the other after the trimming of oligosaccharides by Golgi mannosidases. Certain of the chimeras differed from HA in their ability to pass through each of these steps. Replacement of the HA transmembrane domain with the analogous sequences from other proteins affected folding and transport of the chimeric HAs in ways that suggest that the HA transmembrane sequences form a specific structure in the membrane that differs from that formed by analogous sequences from the other proteins.

AB - Eleven chimeric proteins were created in which the transmembrane, the cytoplasmic, or both topological domains of the influenza virus hemagglutinin (HA) were replaced with those from five other glycoproteins. All of the chimeric HAs reached the cell surface but appeared to differ in the degree to which they were stably folded. Comparisons of the rates of folding, passage into the Golgi, and arrival at the plasma membrane of wild-type HA and the chimeric proteins suggest that formation of a stable HA trimer is not an absolute requirement for export from the endoplasmic reticulum. In addition, there appear to be at least two steps at which the rate of transport can be altered during exocytosis, one occurring before and the other after the trimming of oligosaccharides by Golgi mannosidases. Certain of the chimeras differed from HA in their ability to pass through each of these steps. Replacement of the HA transmembrane domain with the analogous sequences from other proteins affected folding and transport of the chimeric HAs in ways that suggest that the HA transmembrane sequences form a specific structure in the membrane that differs from that formed by analogous sequences from the other proteins.

UR - http://www.scopus.com/inward/record.url?scp=0025239640&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025239640&partnerID=8YFLogxK

M3 - Article

C2 - 2307684

AN - SCOPUS:0025239640

VL - 265

SP - 4760

EP - 4767

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 8

ER -