Molecular cloning and characterization of Dr-II, a nonfimbrial adhesin- i-like adhesin isolated from gestational pyelonephritis-associated Escherichia coli that binds to decay-accelerating factor

Tuan Q. Pham, Pawel Goluszko, Vsevolod Popov, Stella Nowicki, Bogdan J. Nowicki

Research output: Contribution to journalArticle

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Abstract

Bacterial adhesins play an important role in the colonization of the human urogenital tract. Escherichia coli Dr family adhesins have been found to be frequently expressed in strains associated with pyelonephritis in pregnant females. The tissue receptor for known Dr adhesins has been localized to the short consensus repeat-3 (SCR-3) domain of decay accelerating factor (DAF), a complement regulatory protein. In this report, we identified and cloned draE2, a gene encoding a novel 17-kDa DAF-binding adhesin, Dr-II, from a strain of E. coli associated with acute gestational pyelonephritis. Despite the significant sequence diversity between Dr-II and Dr family adhesins, the receptor of Dr-II was found to be the SCR-3 domain of DAF. Sequence analysis of the 186-amino-acid Dr-II open reading frame revealed significant diversity from other members of the Dr adhesin family, including Dr, AFA-I, AFA-III, and F1845, but only an 8-amino-acid difference in sequence from that of the 17-kDa nonfimbrial adhesin NFA-I of unknown receptor specificity. N-terminal peptide sequencing of the purified adhesin confirmed the identity of the open reading frame and indicated cleavage of a 28-amino-acid signal peptide. Antibodies raised against purified Dr-II adhesin exhibited little or no cross-reactivity to Dr adhesin. Characterization of the biological properties demonstrated that like the Dr adhesins, Dr-II was associated with the ability of E. coli to bind to tubular basement membranes and Bowman's capsule and to be internalized into HeLa cells.

Original languageEnglish (US)
Pages (from-to)4309-4318
Number of pages10
JournalInfection and Immunity
Volume65
Issue number10
StatePublished - Oct 1997

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CD55 Antigens
Pyelonephritis
Molecular Cloning
Escherichia coli
Open Reading Frames
Bacterial Adhesins
Bowman Capsule
Amino Acids
Protein Sequence Analysis
Protein Sorting Signals
HeLa Cells
Basement Membrane
Complement System Proteins
Peptides
Antibodies
Genes

ASJC Scopus subject areas

  • Immunology

Cite this

Molecular cloning and characterization of Dr-II, a nonfimbrial adhesin- i-like adhesin isolated from gestational pyelonephritis-associated Escherichia coli that binds to decay-accelerating factor. / Pham, Tuan Q.; Goluszko, Pawel; Popov, Vsevolod; Nowicki, Stella; Nowicki, Bogdan J.

In: Infection and Immunity, Vol. 65, No. 10, 10.1997, p. 4309-4318.

Research output: Contribution to journalArticle

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abstract = "Bacterial adhesins play an important role in the colonization of the human urogenital tract. Escherichia coli Dr family adhesins have been found to be frequently expressed in strains associated with pyelonephritis in pregnant females. The tissue receptor for known Dr adhesins has been localized to the short consensus repeat-3 (SCR-3) domain of decay accelerating factor (DAF), a complement regulatory protein. In this report, we identified and cloned draE2, a gene encoding a novel 17-kDa DAF-binding adhesin, Dr-II, from a strain of E. coli associated with acute gestational pyelonephritis. Despite the significant sequence diversity between Dr-II and Dr family adhesins, the receptor of Dr-II was found to be the SCR-3 domain of DAF. Sequence analysis of the 186-amino-acid Dr-II open reading frame revealed significant diversity from other members of the Dr adhesin family, including Dr, AFA-I, AFA-III, and F1845, but only an 8-amino-acid difference in sequence from that of the 17-kDa nonfimbrial adhesin NFA-I of unknown receptor specificity. N-terminal peptide sequencing of the purified adhesin confirmed the identity of the open reading frame and indicated cleavage of a 28-amino-acid signal peptide. Antibodies raised against purified Dr-II adhesin exhibited little or no cross-reactivity to Dr adhesin. Characterization of the biological properties demonstrated that like the Dr adhesins, Dr-II was associated with the ability of E. coli to bind to tubular basement membranes and Bowman's capsule and to be internalized into HeLa cells.",
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