Deletion and duplication of specific sequences in the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli

Research output: Contribution to journal › Journal article › Research › peer-review

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Deletion and duplication of specific sequences in the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. / Pedersen, Per Amstrup; Andersen, Lene Nonboe.

In: MGG Molecular & General Genetics, Vol. 229, No. 2, 01.10.1991, p. 285-291.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Pedersen, PA & Andersen, LN 1991, 'Deletion and duplication of specific sequences in the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli', MGG Molecular & General Genetics, vol. 229, no. 2, pp. 285-291. https://doi.org/10.1007/BF00272168

APA

Pedersen, P. A., & Andersen, L. N. (1991). Deletion and duplication of specific sequences in the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. MGG Molecular & General Genetics, 229(2), 285-291. https://doi.org/10.1007/BF00272168

Vancouver

Pedersen PA, Andersen LN. Deletion and duplication of specific sequences in the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. MGG Molecular & General Genetics. 1991 Oct 1;229(2):285-291. https://doi.org/10.1007/BF00272168

Author

Pedersen, Per Amstrup ; Andersen, Lene Nonboe. / Deletion and duplication of specific sequences in the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. In: MGG Molecular & General Genetics. 1991 ; Vol. 229, No. 2. pp. 285-291.

Bibtex

@article{18b51de059354750adf7eff7f911d6e6,
title = "Deletion and duplication of specific sequences in the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli",
abstract = "Small, defined in-frame deletions and in-frame duplications of specific sequences were made within the faeG gene encoding the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. The cellular localization and proteolytic stability of the different mutated fimbrial subunit proteins were determined, and compared with those of the wild-type protein. Based upon these results, we predict a functional role of specific structures in the K88ab fimbrial subunit protein in subunit-subunit interactions as well as in interactions between FaeG and the other proteins encoded by the K88ab operon. The results obtained were further compared with results obtained from operon deletions, linker insertion mutagenesis and the current model for biogenesis of K88 fimbriae. One of the mutated fimbrial subunit genes was used to construct a secreted in-frame fusion between FaeG and a characterized epitope (lacking cysteine) from the Hepatitis B pre-S2 protein. Such fusion proteins might be useful in the design of recombinant vaccines.",
keywords = "Escherichia coli, K88 fimbriae, Organelle assembly, Protein secretion",
author = "Pedersen, {Per Amstrup} and Andersen, {Lene Nonboe}",
year = "1991",
month = oct,
day = "1",
doi = "10.1007/BF00272168",
language = "English",
volume = "229",
pages = "285--291",
journal = "Molecular General Genetics",
issn = "0026-8925",
publisher = "Springer Verlag",
number = "2",

}

RIS

TY - JOUR

T1 - Deletion and duplication of specific sequences in the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli

AU - Pedersen, Per Amstrup

AU - Andersen, Lene Nonboe

PY - 1991/10/1

Y1 - 1991/10/1

N2 - Small, defined in-frame deletions and in-frame duplications of specific sequences were made within the faeG gene encoding the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. The cellular localization and proteolytic stability of the different mutated fimbrial subunit proteins were determined, and compared with those of the wild-type protein. Based upon these results, we predict a functional role of specific structures in the K88ab fimbrial subunit protein in subunit-subunit interactions as well as in interactions between FaeG and the other proteins encoded by the K88ab operon. The results obtained were further compared with results obtained from operon deletions, linker insertion mutagenesis and the current model for biogenesis of K88 fimbriae. One of the mutated fimbrial subunit genes was used to construct a secreted in-frame fusion between FaeG and a characterized epitope (lacking cysteine) from the Hepatitis B pre-S2 protein. Such fusion proteins might be useful in the design of recombinant vaccines.

AB - Small, defined in-frame deletions and in-frame duplications of specific sequences were made within the faeG gene encoding the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. The cellular localization and proteolytic stability of the different mutated fimbrial subunit proteins were determined, and compared with those of the wild-type protein. Based upon these results, we predict a functional role of specific structures in the K88ab fimbrial subunit protein in subunit-subunit interactions as well as in interactions between FaeG and the other proteins encoded by the K88ab operon. The results obtained were further compared with results obtained from operon deletions, linker insertion mutagenesis and the current model for biogenesis of K88 fimbriae. One of the mutated fimbrial subunit genes was used to construct a secreted in-frame fusion between FaeG and a characterized epitope (lacking cysteine) from the Hepatitis B pre-S2 protein. Such fusion proteins might be useful in the design of recombinant vaccines.

KW - Escherichia coli

KW - K88 fimbriae

KW - Organelle assembly

KW - Protein secretion

UR - http://www.scopus.com/inward/record.url?scp=0025954246&partnerID=8YFLogxK

U2 - 10.1007/BF00272168

DO - 10.1007/BF00272168

M3 - Journal article

C2 - 1681414

AN - SCOPUS:0025954246

VL - 229

SP - 285

EP - 291

JO - Molecular General Genetics

JF - Molecular General Genetics

SN - 0026-8925

IS - 2

ER -

ID: 227044280