An efficient method to express GPI-anchor proteins in insect cells

Hosam Shams-Eldin; Nahid Azzouz; Sebastian Niehus; Terry K. Smith; Ralph T. Schwarz

doi:10.1016/j.bbrc.2007.11.026

An efficient method to express GPI-anchor proteins in insect cells

Hosam Shams-Eldin, Nahid Azzouz, Sebastian Niehus, Terry K. Smith, Ralph T. Schwarz

Research output: Contribution to journal › Article › peer-review

Abstract

Glycosylphosphatidylinositols (GPIs) constitute a class of glycolipids that have various functions, the most basic being to attach proteins to the surface of eukaryotic cells. GPIs have to be taken into account, when expressing surface antigens from parasitic protozoa in heterologous systems. The synthesis of the GPI-anchors was previously reported to be drastically decreased to almost background level following baculovirus infection. Here we describe a new method to express GPI-anchor proteins in insect cells relying on using of a supplementary baculovirus construct that overexpresses the N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the enzyme catalyzing the second step in the GPI biosynthetic pathway. (c) 2007 Elsevier Inc. All rights reserved.

Original language	English
Pages (from-to)	657-663
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	365
DOIs	https://doi.org/10.1016/j.bbrc.2007.11.026
Publication status	Published - 25 Jan 2008

Keywords

baculovirus
insect cells
Sf9
high five
glycosylphosphatidylinositols
N-glycosylation
toxoplasma gondii
N-acetylglucosaminyl phosphatidylinositol de-n-acetylase
PIGL
SAG1
MEROZOITE SURFACE PROTEIN-1
GLYCOSYLPHOSPHATIDYLINOSITOL BIOSYNTHETIC-PATHWAY
DE-N-ACETYLASE
PLASMODIUM-FALCIPARUM
RECOMBINANT GLYCOPROTEINS
INHIBITORY ANTIBODIES
BACULOVIRUS INFECTION
TRYPANOSOMA-BRUCEI
TOXOPLASMA-GONDII
MAMMALIAN-CELLS

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10.1016/j.bbrc.2007.11.026

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title = "An efficient method to express GPI-anchor proteins in insect cells",

abstract = "Glycosylphosphatidylinositols (GPIs) constitute a class of glycolipids that have various functions, the most basic being to attach proteins to the surface of eukaryotic cells. GPIs have to be taken into account, when expressing surface antigens from parasitic protozoa in heterologous systems. The synthesis of the GPI-anchors was previously reported to be drastically decreased to almost background level following baculovirus infection. Here we describe a new method to express GPI-anchor proteins in insect cells relying on using of a supplementary baculovirus construct that overexpresses the N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the enzyme catalyzing the second step in the GPI biosynthetic pathway. (c) 2007 Elsevier Inc. All rights reserved.",

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author = "Hosam Shams-Eldin and Nahid Azzouz and Sebastian Niehus and Smith, {Terry K.} and Schwarz, {Ralph T.}",

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doi = "10.1016/j.bbrc.2007.11.026",

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T1 - An efficient method to express GPI-anchor proteins in insect cells

AU - Shams-Eldin, Hosam

AU - Azzouz, Nahid

AU - Niehus, Sebastian

AU - Smith, Terry K.

AU - Schwarz, Ralph T.

PY - 2008/1/25

Y1 - 2008/1/25

N2 - Glycosylphosphatidylinositols (GPIs) constitute a class of glycolipids that have various functions, the most basic being to attach proteins to the surface of eukaryotic cells. GPIs have to be taken into account, when expressing surface antigens from parasitic protozoa in heterologous systems. The synthesis of the GPI-anchors was previously reported to be drastically decreased to almost background level following baculovirus infection. Here we describe a new method to express GPI-anchor proteins in insect cells relying on using of a supplementary baculovirus construct that overexpresses the N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the enzyme catalyzing the second step in the GPI biosynthetic pathway. (c) 2007 Elsevier Inc. All rights reserved.

AB - Glycosylphosphatidylinositols (GPIs) constitute a class of glycolipids that have various functions, the most basic being to attach proteins to the surface of eukaryotic cells. GPIs have to be taken into account, when expressing surface antigens from parasitic protozoa in heterologous systems. The synthesis of the GPI-anchors was previously reported to be drastically decreased to almost background level following baculovirus infection. Here we describe a new method to express GPI-anchor proteins in insect cells relying on using of a supplementary baculovirus construct that overexpresses the N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the enzyme catalyzing the second step in the GPI biosynthetic pathway. (c) 2007 Elsevier Inc. All rights reserved.

KW - baculovirus

KW - insect cells

KW - Sf9

KW - high five

KW - glycosylphosphatidylinositols

KW - N-glycosylation

KW - toxoplasma gondii

KW - N-acetylglucosaminyl phosphatidylinositol de-n-acetylase

KW - PIGL

KW - SAG1

KW - MEROZOITE SURFACE PROTEIN-1

KW - GLYCOSYLPHOSPHATIDYLINOSITOL BIOSYNTHETIC-PATHWAY

KW - DE-N-ACETYLASE

KW - PLASMODIUM-FALCIPARUM

KW - RECOMBINANT GLYCOPROTEINS

KW - INHIBITORY ANTIBODIES

KW - BACULOVIRUS INFECTION

KW - TRYPANOSOMA-BRUCEI

KW - TOXOPLASMA-GONDII

KW - MAMMALIAN-CELLS

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U2 - 10.1016/j.bbrc.2007.11.026

DO - 10.1016/j.bbrc.2007.11.026

M3 - Article

SN - 0006-291X

VL - 365

SP - 657

EP - 663

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

ER -

An efficient method to express GPI-anchor proteins in insect cells

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Keywords

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