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(Received for publication, October 16, 1995; and in revised form, January 16, 1996) Acid phosphatases (Acp) of intracellular pathogens have recently
been implicated as virulence factors that enhance intracellular
survival through suppression of the respiratory burst. We describe here
the identification, purification, characterization, and sequencing of a
novel burst-inhibiting acid phosphatase from the facultative
intracellular bacterium, Francisella tularensis. Similar to
other the burst-inhibiting Acps, F. tularensis Acp (AcpA) is
tartrate-resistant and has broad substrate specificity. The AcpA enzyme
is unique, however, in that it is easily released from the bacterial
cell in soluble form, is a basic enzyme, suppresses the respiratory
burst of not only fMet-Leu-Phe but also phorbol 12-myristate
13-acetate-stimulated neutrophils and does not fit into any of the
three currently recognized classes of acid phosphatase. We also report
the complete nucleotide sequence of the gene acpA, encoding
AcpA, and the deduced primary structure of its encoded polypeptide.
Comparative sequence analyses of AcpA is discussed. To our knowledge,
this is the first report describing the cloning and sequencing of a
burst-inhibiting acid phosphatase.
Volume 271,
Number 18,
Issue of May 3, 1996 pp. 10973-10983
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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