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Identification and characterization of the acid phosphatase from Francisella tularensis and its potential role in pathogenesis

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Title: Identification and characterization of the acid phosphatase from Francisella tularensis and its potential role in pathogenesis
Author(s): Reilly, Thomas James
Doctoral Committee Chair(s): Kuhlenschmidt, Mark S.
Department / Program: Pathobiology
Discipline: Pathobiology
Degree Granting Institution: University of Illinois at Urbana-Champaign
Degree: Ph.D.
Genre: Dissertation
Subject(s): Biology, Microbiology Agriculture, Animal Pathology Biology, Veterinary Science
Abstract: Successful intracellular pathogens resist or prevent the formation of antimicrobial substances produced by professional phagocytes including, toxic oxygen intermediates of the respiratory burst. Purified acid phosphatases (ACP) from Leishmania donovani and Legionella micdadei have been shown to cause the dose dependent suppression of the respiratory burst (Remaley et al., 1984 and Saha et al., 1985). Depression of the respiratory burst by phosphatase-catalyzed dephosphorylation of phosphatidylinositol 4,5-bisphosphate and inositol 1,4,5-trisphosphate is believed to play an important role in the intracellular survival of these pathogens. Results from this study show that the intracellular pathogen, F. tularensis (Ft) produces a respiratory burst-inhibiting acid phosphatase. The acid phosphatase appears to be identical in three strains tested. Like many microbial acid phosphatases, FtACP has been localized to the periplasmic space of the organism. FtACP has the following properties: molecular mass $\sim$56 kDa, pH optimum of 6.0 for five different substrates, isoelectric point of 9.2, broad substrate specificity including. The enzyme was inhibited by molybdate, vanadate, and mercury but was resistant to scL-(+) tartrate, fluoride, chelators of divalent cations, and okadaic acid. FtACP possesses protein tyrosyl phosphatase activity when incubated in the presence of the monophosphorylated peptide p60$\sp{\rm src}$. Another unusual property of this bacterial phosphatase is that it appears to possess covalently associated carbohydrates tentatively identified as glucose, mannose, and galactose. Like other burst inhibiting acid phosphatases, this enzyme caused the dose dependent suppression of fMLP stimulated neutrophils and displayed maximum effects on the respiratory burst after a 15 minute pre-incubation period. Unlike other respiratory burst-inhibiting acid phosphatases, FtACP inhibited the respiratory burst of PMA stimulated neutrophils. Preliminary evidence also suggests FtACP may inhibit the expansion of Con A stimulated T cells. These data are consistent with the hypothesis that FtACP plays a role in the survival and virulence of this pathogen. Another interesting aspect of this study is that FtACP cannot equivocally be classified into any of the existing classes of acid phosphatases. This conclusion may be a consequence of the dual role for this enzyme: intracellular survival and axenic growth.
Issue Date: 1994
Type: Text
Language: English
URI: http://hdl.handle.net/2142/22043
Rights Information: Copyright 1994 Reilly, Thomas James
Date Available in IDEALS: 2011-05-07
Identifier in Online Catalog: AAI9512526
OCLC Identifier: (UMI)AAI9512526
 

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