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Infection and Immunity, December 2001, p. 7293-7303, Vol. 69, No. 12
Department of Biochemistry and Molecular
Biology, Penn State College of Medicine, Hershey, Pennsylvania 17033
Received 14 June 2001/Returned for modification 16 August
2001/Accepted 6 September 2001
The eib genes of Escherichia coli
encode surface-exposed proteins which bind immunoglobulins (Ig) such as
the Fc fragment of human IgG (IgG Fc) in a nonimmune manner. The
Eib proteins belong to a family which includes YadA of
Yersinia, UspA2 of Moraxella, and DsrA of
Haemophilus ducreyi. This family of surface-exposed proteins shares several features, such as the ability to impart resistance to human serum complement and a tendency to exist as stable
multimers. Four genes, eibA, eibC,
eibD and eibE, were previously identified
and cloned from ECOR-9, a strain from the E. coli
reference collection. EibC, -D, and -E bind human serum IgA in addition
to IgG, but no IgA binding has been observed for EibA. Here, we report
the cloning of a new eib gene, eibF, from a second strain of E. coli, ECOR-2. The product, EibF,
has a relatively strong preference for IgA. Like the other
eib genes, eibF attenuates serum
sensitivity, occurs as a stable multimer, and is associated with
a prophage. By subcloning portions of the eibA and
eibF genes, we have identified distinct sequence
segments sufficient to cause Ig binding, multimerization, and
discrimination between IgA and IgG. The ability to multimerize is
associated with a sequence close to the C terminus that is homologous
to other family members such as YadA. Binding of IgG Fc is associated
with a sequence that is highly conserved among all Eib proteins but
otherwise unique. Binding of IgA is associated with a sequence of EibF
that is not similar to any EibA sequence.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.12.7293-7203.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Nonimmune Binding of Human Immunoglobulin A (IgA)
and IgG Fc by Distinct Sequence Segments of the EibF Cell Surface
Protein of Escherichia coli
*
Corresponding author. Mailing address: Department of
Biochemistry and Molecular Biology, Pennsylvania State College of
Medicine, Mail Services H171, Hershey, PA 17033-0850. Phone: (717)
284-2881. Fax: (717) 531-7072. E-mail: csandt{at}psu.edu.
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