Low molecular weight high-mannose type glycans in a secreted protein of the filamentous fungus Trichoderma reesei

Irma Salovuori, Marja Makarow, Heikki Rauvala, Jonathan Knowles, Leevi Kääriäinen

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

With the object of obtaining information about the suitability of filamentous fungi for production of heterogeneous mammalian proteins, we have characterized the normal glycosylation pattern of CBH I, the major glycoprotein secreted by Trichoderma reesei.
The protein–bound glycans of CBH I were studied using a variety of separation techniques to analyze the products of specific glycosidase digestions and chemical degradation procedures. CBH I contains both O–glycosidic and N–glycosidic glycans.
The O–glycosidic glycans consist of one to four hexose residues which are mostly mannose. The structures of the N–glycosidic glycans are (Man)5(GlcNAc)2 and (Man)9(GlcNAc)2.
Thus it may be possible to use T. reesei as a host for the production of heterologous glycoproteins of animal origin, and to take advantage of its remarkable secretory capacity.
Original languageEnglish
Pages (from-to)152-156
JournalBio/Technology
Volume5
Issue number2
DOIs
Publication statusPublished - 1987
MoE publication typeA1 Journal article-refereed

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Glycoproteins
Trichoderma
Mannose
Fungi
Polysaccharides
Molecular Weight
Molecular weight
Glycosylation
Proteins
Animals
Degradation
Hexoses
Glycoside Hydrolases
Digestion

Cite this

Salovuori, Irma ; Makarow, Marja ; Rauvala, Heikki ; Knowles, Jonathan ; Kääriäinen, Leevi. / Low molecular weight high-mannose type glycans in a secreted protein of the filamentous fungus Trichoderma reesei. In: Bio/Technology. 1987 ; Vol. 5, No. 2. pp. 152-156.
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title = "Low molecular weight high-mannose type glycans in a secreted protein of the filamentous fungus Trichoderma reesei",
abstract = "With the object of obtaining information about the suitability of filamentous fungi for production of heterogeneous mammalian proteins, we have characterized the normal glycosylation pattern of CBH I, the major glycoprotein secreted by Trichoderma reesei. The protein–bound glycans of CBH I were studied using a variety of separation techniques to analyze the products of specific glycosidase digestions and chemical degradation procedures. CBH I contains both O–glycosidic and N–glycosidic glycans. The O–glycosidic glycans consist of one to four hexose residues which are mostly mannose. The structures of the N–glycosidic glycans are (Man)5(GlcNAc)2 and (Man)9(GlcNAc)2. Thus it may be possible to use T. reesei as a host for the production of heterologous glycoproteins of animal origin, and to take advantage of its remarkable secretory capacity.",
author = "Irma Salovuori and Marja Makarow and Heikki Rauvala and Jonathan Knowles and Leevi K{\"a}{\"a}ri{\"a}inen",
year = "1987",
doi = "10.1038/nbt0287-152",
language = "English",
volume = "5",
pages = "152--156",
journal = "Nature Biotechnology",
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Salovuori, I, Makarow, M, Rauvala, H, Knowles, J & Kääriäinen, L 1987, 'Low molecular weight high-mannose type glycans in a secreted protein of the filamentous fungus Trichoderma reesei', Bio/Technology, vol. 5, no. 2, pp. 152-156. https://doi.org/10.1038/nbt0287-152

Low molecular weight high-mannose type glycans in a secreted protein of the filamentous fungus Trichoderma reesei. / Salovuori, Irma; Makarow, Marja; Rauvala, Heikki; Knowles, Jonathan; Kääriäinen, Leevi.

In: Bio/Technology, Vol. 5, No. 2, 1987, p. 152-156.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Low molecular weight high-mannose type glycans in a secreted protein of the filamentous fungus Trichoderma reesei

AU - Salovuori, Irma

AU - Makarow, Marja

AU - Rauvala, Heikki

AU - Knowles, Jonathan

AU - Kääriäinen, Leevi

PY - 1987

Y1 - 1987

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AB - With the object of obtaining information about the suitability of filamentous fungi for production of heterogeneous mammalian proteins, we have characterized the normal glycosylation pattern of CBH I, the major glycoprotein secreted by Trichoderma reesei. The protein–bound glycans of CBH I were studied using a variety of separation techniques to analyze the products of specific glycosidase digestions and chemical degradation procedures. CBH I contains both O–glycosidic and N–glycosidic glycans. The O–glycosidic glycans consist of one to four hexose residues which are mostly mannose. The structures of the N–glycosidic glycans are (Man)5(GlcNAc)2 and (Man)9(GlcNAc)2. Thus it may be possible to use T. reesei as a host for the production of heterologous glycoproteins of animal origin, and to take advantage of its remarkable secretory capacity.

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JO - Nature Biotechnology

JF - Nature Biotechnology

SN - 1087-0156

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