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Infection and Immunity, September 2000, p. 5210-5217, Vol. 68, No. 9
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Diversity of ace, a Gene Encoding a Microbial Surface
Component Recognizing Adhesive Matrix Molecules, from Different Strains
of Enterococcus faecalis and Evidence for Production
of Ace during Human Infections
Sreedhar R.
Nallapareddy,1,2
Kavindra V.
Singh,1,2
Ruay-Wang
Duh,1,2,
George M.
Weinstock,2,3 and
Barbara E.
Murray1,2,3,*
Division of Infectious Diseases, Department
of Internal Medicine,1 Center for the
Study of Emerging and Re-emerging
Pathogens,2 and Department of
Microbiology and Molecular Genetics,3
University of Texas Medical School, Houston, Texas 77030
Received 10 April 2000/Returned for modification 12 May
2000/Accepted 16 June 2000
Our previous work reported that most Enterococcus
faecalis strains adhered to the extracellular matrix proteins
collagen types I and IV and laminin after growth at 46°C, but not
37°C, and we subsequently identified an E. faecalis
sequence, ace, that encodes a bacterial adhesin similar to
the collagen binding protein Cna of Staphylococcus aureus.
In this study, we examined the diversity of E. faecalis-specific ace gene sequences among different
isolates obtained from various geographic regions as well as from
various clinical sources. A comparison of nucleotide and deduced amino acid sequences of Ace from nine E. faecalis strains
identified a highly conserved N-terminal A domain, followed by a
variable B domain which contains two to five repeats of 47 amino acids in tandem array, preceded by a 20-amino-acid partial repeat. Using 17 other strains collected worldwide, the 5' region of ace
that encodes the A domain was sequenced, and these sequences showed
97.5% identity. Among the previously reported five amino acids critical for collagen binding by Cna of S. aureus, four
were found to be identical in Ace from all strains tested. Polyclonal
immune rabbit serum prepared against recombinant Ace A derived from
E. faecalis strain OG1RF detected Ace in mutanolysin
extracts of seven of nine E. faecalis strains after growth
at 46°C; Ace was detected in four different molecular sizes that
correspond to the variation in the B repeat region. To determine if
there was any evidence to indicate that Ace might be produced under
physiological conditions, we quantitatively assayed sera collected from
patients with enterococcal infections for the presence of anti-Ace A
antibodies. Ninety percent of sera (19 of 21) from patients with
E. faecalis endocarditis showed reactivity with titers from
1:32 to >1:1,024; the only 2 sera which lacked antibodies to Ace A had
considerably lower titers of antibodies to other E. faecalis antigens as well. Human-derived, anti-Ace A
immunoglobulins G purified from an E. faecalis endocarditis
patient serum inhibited adherence of 46°C-grown E. faecalis OG1RF to collagen types I and IV and laminin. In
conclusion, these results show that ace is highly conserved
among isolates of E. faecalis, with at least four variants
related to the differences in the B domain, is expressed by different
strains during infection in humans, and human-derived antibodies can
block adherence to these extracellular matrix proteins.
*
Corresponding author. Mailing address: Center for the
Study of Emerging and Re-emerging Pathogens, Division of Infectious Diseases, Department of Internal Medicine, University of Texas Medical
School at Houston, 6431 Fannin St., Houston, TX 77030. Phone: (713)
500-6767. Fax: (713) 500-5495. E-mail:
infdis{at}heart.med.uth.tmc.edu.

Present address: Section of Infectious Diseases, Department of
Medicine, Veterans General Hospital

Taipei, Taipei, Taiwan,
Republic
of
China.
Infection and Immunity, September 2000, p. 5210-5217, Vol. 68, No. 9
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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