Lectin-Resistant CHO Glycosylation Mutants

Santosh Kumar Patnaik, Pamela Stanley

Research output: Contribution to journalArticle

130 Citations (Scopus)

Abstract

Chinese hamster ovary (CHO) mutant cells with a wide variety of alterations in the glycosylation of proteins and lipids have been isolated by selection for resistance to the cytotoxicity of plant lectins. These CHO mutants have been used to characterize glycosylation pathways, to identify genes that code for glycosylation activities, to elucidate functional roles of glycans that mediate biological processes, and for glycosylation engineering. In this chapter, we briefly describe the available panel of lectin-resistant CHO mutants and summarize their glycan alterations and the biochemical and genetic bases of mutation.

Original languageEnglish (US)
Pages (from-to)159-182
Number of pages24
JournalMethods in Enzymology
Volume416
DOIs
StatePublished - 2006
Externally publishedYes

Fingerprint

Glycosylation
Cricetulus
Lectins
Ovary
Polysaccharides
Plant Lectins
Biological Phenomena
Cytotoxicity
Molecular Biology
Genes
Lipids
Mutation
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Lectin-Resistant CHO Glycosylation Mutants. / Patnaik, Santosh Kumar; Stanley, Pamela.

In: Methods in Enzymology, Vol. 416, 2006, p. 159-182.

Research output: Contribution to journalArticle

Patnaik, Santosh Kumar ; Stanley, Pamela. / Lectin-Resistant CHO Glycosylation Mutants. In: Methods in Enzymology. 2006 ; Vol. 416. pp. 159-182.
@article{f7afe91d9b6140939ca2dea52cb8dce5,
title = "Lectin-Resistant CHO Glycosylation Mutants",
abstract = "Chinese hamster ovary (CHO) mutant cells with a wide variety of alterations in the glycosylation of proteins and lipids have been isolated by selection for resistance to the cytotoxicity of plant lectins. These CHO mutants have been used to characterize glycosylation pathways, to identify genes that code for glycosylation activities, to elucidate functional roles of glycans that mediate biological processes, and for glycosylation engineering. In this chapter, we briefly describe the available panel of lectin-resistant CHO mutants and summarize their glycan alterations and the biochemical and genetic bases of mutation.",
author = "Patnaik, {Santosh Kumar} and Pamela Stanley",
year = "2006",
doi = "10.1016/S0076-6879(06)16011-5",
language = "English (US)",
volume = "416",
pages = "159--182",
journal = "ImmunoMethods",
issn = "1046-2023",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Lectin-Resistant CHO Glycosylation Mutants

AU - Patnaik, Santosh Kumar

AU - Stanley, Pamela

PY - 2006

Y1 - 2006

N2 - Chinese hamster ovary (CHO) mutant cells with a wide variety of alterations in the glycosylation of proteins and lipids have been isolated by selection for resistance to the cytotoxicity of plant lectins. These CHO mutants have been used to characterize glycosylation pathways, to identify genes that code for glycosylation activities, to elucidate functional roles of glycans that mediate biological processes, and for glycosylation engineering. In this chapter, we briefly describe the available panel of lectin-resistant CHO mutants and summarize their glycan alterations and the biochemical and genetic bases of mutation.

AB - Chinese hamster ovary (CHO) mutant cells with a wide variety of alterations in the glycosylation of proteins and lipids have been isolated by selection for resistance to the cytotoxicity of plant lectins. These CHO mutants have been used to characterize glycosylation pathways, to identify genes that code for glycosylation activities, to elucidate functional roles of glycans that mediate biological processes, and for glycosylation engineering. In this chapter, we briefly describe the available panel of lectin-resistant CHO mutants and summarize their glycan alterations and the biochemical and genetic bases of mutation.

UR - http://www.scopus.com/inward/record.url?scp=33751002037&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33751002037&partnerID=8YFLogxK

U2 - 10.1016/S0076-6879(06)16011-5

DO - 10.1016/S0076-6879(06)16011-5

M3 - Article

C2 - 17113866

AN - SCOPUS:33751002037

VL - 416

SP - 159

EP - 182

JO - ImmunoMethods

JF - ImmunoMethods

SN - 1046-2023

ER -