Functional phytohemagglutinin (PHA) and Galanthus nivalis agglutinin (GNA) expressed in Pichia pastoris . Correct N-terminal processing and secretion of heterologous proteins expressed using the PHA-E signal peptide

The methanol-utilizing yeast Pichia pastoris has been developed as a host system for the production of heterologous proteins of commercial interest. An industrial yeast selected for efficient growth on methanol for biomass generation, P. pastoris is readily grown on defined medium in continuous culture at high volume and density. A unique feature of the expression system is the promoter employed to drive heterologous gene expression, which is derived from the methanol-regulated alcohol oxidase I gene (AOX1) of P. pastoris, one of the most efficient and tightly regulated promoters known. The strength of the AOX1 promoter results in high expression levels in strains harboring only a single integrated copy of a foreign-gene expression cassette. Levels may often be further enhanced through the integration of multiple cassette copies into the P. pastoris genome and strategies to construct and select multicopy cassette strains have been devised. The system is particularly attractive for the secretion of foreign-gene products. Because P. pastoris endogenous protein secretion levels are low, foreign secreted proteins often appear to be virtually the only proteins in the culture broth, a major advantage in processing and purification. Key words: heterologous gene expression, methylotrophic yeast, Pichia pastoris, secretion, glycosylation.

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Process Technology for Production and Recovery of Heterologous Proteins with Pichia pastoris

Biotechnology Progress ◽

10.1021/bp060171t ◽

2006 ◽

Vol 22 (6) ◽

pp. 1465-1473 ◽

Cited By ~ 9

Author(s):

M. Jahic ◽

A. Veide ◽

T. Charoenrat ◽

T. Teeri ◽

S.-O. Enfors

Keyword(s):

Pichia Pastoris ◽

Heterologous Proteins ◽

Process Technology

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Comparison of Alpha-Factor Preprosequence and a Classical Mammalian Signal Peptide for Secretion of Recombinant Xylanase xynB from Yeast Pichia pastoris

Journal of Microbiology and Biotechnology ◽

10.4014/jmb.1109.09031 ◽

2012 ◽

Vol 22 (4) ◽

pp. 479-483 ◽

Cited By ~ 13

Author(s):

Zuyong He

Keyword(s):

Pichia Pastoris ◽

Signal Peptide ◽

Yeast Pichia Pastoris ◽

Alpha Factor

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Impact of snowdrop lectin (Galanthus nivalis agglutinin; GNA) on adults of the green lacewing, Chrysoperla carnea

Journal of Insect Physiology ◽

10.1016/j.jinsphys.2008.10.015 ◽

2009 ◽

Vol 55 (2) ◽

pp. 136-143 ◽

Cited By ~ 13

Author(s):

Yunhe Li ◽

Jörg Romeis

Keyword(s):

Chrysoperla Carnea ◽

Green Lacewing ◽

Galanthus Nivalis Agglutinin ◽

Galanthus Nivalis

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Direct and indirect sublethal effects of Galanthus nivalis agglutinin (GNA) on the development of a potato-aphid parasitoid, Aphelinus abdominalis (Hymenoptera: Aphelinidae)

Journal of Insect Physiology ◽

10.1016/s0022-1910(00)00148-7 ◽

2001 ◽

Vol 47 (6) ◽

pp. 553-561 ◽

Cited By ~ 55

Author(s):

Aude Couty ◽

Gloria de la Viña ◽

Suzanne J Clark ◽

Laure Kaiser ◽

M.-H Pham-Delègue ◽

...

Keyword(s):

Sublethal Effects ◽

Aphid Parasitoid ◽

Potato Aphid ◽

Galanthus Nivalis Agglutinin ◽

Galanthus Nivalis

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Characterization of the ToxB Gene from Pyrenophora tritici-repentis

Molecular Plant-Microbe Interactions ◽

10.1094/mpmi.2001.14.5.675 ◽

2001 ◽

Vol 14 (5) ◽

pp. 675-677 ◽

Cited By ~ 57

Author(s):

J. Patrick Martinez ◽

Sean A. Ottum ◽

Shaukat Ali ◽

Leonard J. Francl ◽

Lynda M. Ciuffetti

Keyword(s):

Amino Acid ◽

Pichia Pastoris ◽

Heterologous Expression ◽

North Dakota ◽

Signal Peptide ◽

Open Reading Frame ◽

Reading Frame ◽

Pyrenophora Tritici Repentis ◽

Putative Signal Peptide

The ToxB gene was cloned and characterized from a race 5 isolate of Pyrenophora tritici-repentis from North Dakota. ToxB contains a 261-bp open reading frame that encodes a 23 amino acid putative signal peptide and a 64 amino acid host-selective toxin, Ptr ToxB. Analysis of Ptr ToxB from heterologous expression in Pichia pastoris confirms that ToxB encodes a host-selective toxin.

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