Nonfimbrial blood group N-specific adhesin (NFA-3) from Escherichia coli O20: KX104: H-, causing systemic infection

J. Grünberg; R. Perry; H. Hoschützky; B. Jann; K. Jann; J. Goldhar

doi:10.1111/j.1574-6968.1988.tb03185.x

Nonfimbrial blood group N-specific adhesin (NFA-3) from Escherichia coli O20: KX104: H^-, causing systemic infection

J. Grünberg, R. Perry, H. Hoschützky, B. Jann, K. Jann, J. Goldhar^*

^*Corresponding author for this work

Clinical Microbiology and Immunology

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

12 Scopus citations

Abstract

From unfimbriated Escherichia coli O20 :KX104: H^-, which caused systemic infection in man, and adhesin (NFA-3) was isolated by extraction from the bacteria in phosphate buffered saline at 70°C. It was purified by ammonium sulfate precipitation and anion exchange chromatography in the presence of urea. The adhesin had an apparent molecular weight in excess to 10⁶ daltons and consisted of 17.500-d peptide subunits. It had an isoelectric point of 3.9 and contained one cysteine and no methionine. In haemagglutination assays and adhesion immunoassays, NFA-3 showed a preferred specificity for blood group N.

Original language	English
Pages (from-to)	241-245
Number of pages	5
Journal	FEMS Microbiology Letters
Volume	56
Issue number	2
DOIs	https://doi.org/10.1111/j.1574-6968.1988.tb03185.x
State	Published - 1 Dec 1988

Funding

Funders	Funder number
Ministry of Research and Technology	OI QV 564

Keywords

Blood group N-specific adhesin
Escherichia coli haemagglutinin
Nonfimbrial adhesin

Access to Document

10.1111/j.1574-6968.1988.tb03185.x

Cite this

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title = "Nonfimbrial blood group N-specific adhesin (NFA-3) from Escherichia coli O20: KX104: H-, causing systemic infection",

abstract = "From unfimbriated Escherichia coli O20 :KX104: H-, which caused systemic infection in man, and adhesin (NFA-3) was isolated by extraction from the bacteria in phosphate buffered saline at 70°C. It was purified by ammonium sulfate precipitation and anion exchange chromatography in the presence of urea. The adhesin had an apparent molecular weight in excess to 106 daltons and consisted of 17.500-d peptide subunits. It had an isoelectric point of 3.9 and contained one cysteine and no methionine. In haemagglutination assays and adhesion immunoassays, NFA-3 showed a preferred specificity for blood group N.",

keywords = "Blood group N-specific adhesin, Escherichia coli haemagglutinin, Nonfimbrial adhesin",

author = "J. Gr{\"u}nberg and R. Perry and H. Hosch{\"u}tzky and B. Jann and K. Jann and J. Goldhar",

note = "Funding Information: This work was in part supported by the Ministry of Research and Technology, F.R.G. (BMFT-DFVLZ: OI QV 564).",

year = "1988",

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doi = "10.1111/j.1574-6968.1988.tb03185.x",

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T2 - KX104: H-, causing systemic infection

AU - Grünberg, J.

AU - Perry, R.

AU - Hoschützky, H.

AU - Jann, B.

AU - Jann, K.

AU - Goldhar, J.

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PY - 1988/12/1

Y1 - 1988/12/1

N2 - From unfimbriated Escherichia coli O20 :KX104: H-, which caused systemic infection in man, and adhesin (NFA-3) was isolated by extraction from the bacteria in phosphate buffered saline at 70°C. It was purified by ammonium sulfate precipitation and anion exchange chromatography in the presence of urea. The adhesin had an apparent molecular weight in excess to 106 daltons and consisted of 17.500-d peptide subunits. It had an isoelectric point of 3.9 and contained one cysteine and no methionine. In haemagglutination assays and adhesion immunoassays, NFA-3 showed a preferred specificity for blood group N.

AB - From unfimbriated Escherichia coli O20 :KX104: H-, which caused systemic infection in man, and adhesin (NFA-3) was isolated by extraction from the bacteria in phosphate buffered saline at 70°C. It was purified by ammonium sulfate precipitation and anion exchange chromatography in the presence of urea. The adhesin had an apparent molecular weight in excess to 106 daltons and consisted of 17.500-d peptide subunits. It had an isoelectric point of 3.9 and contained one cysteine and no methionine. In haemagglutination assays and adhesion immunoassays, NFA-3 showed a preferred specificity for blood group N.

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KW - Escherichia coli haemagglutinin

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