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A more recent version of this article appeared on March 1, 2002.
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Submitted on November 19, 2001
Revised on January 15, 2002
Accepted on January 18, 2002

The Rickettsia prowazekii invasion gene homolog (invA) encodes a nudix hydrolase active on adenosine (5')-pentaphospho-(5')-adenosine (Ap5A)

Jariyanart Gaywee, WenLian Xu, Suzana Radulovic, Maurice J. Bessman, and Abdu F. Azad

Microbiology and Immunology, University of Maryland, Baltimore, Baltimore, MD 21201

Corresponding Author: aazad{at}umaryland.edu

The genomic sequence of Rickettsia prowazekii, the obligate intracellular bacterium responsible for epidemic typhus, reveals an uncharacterized invasion gene homolog (invA). The deduced protein of 18,752 Da contains a Nudix signature, the specific motif found in the Nudix hydrolase family. To characterize the function of InvA, the gene was cloned and over- expressed in Escherichia coli. The expressed protein was purified to near homogeneity and subsequently tested for its enzymatic activity against a series of nucleoside diphosphate derivatives. The purified InvA exhibits hydrolytic activity toward dinucleoside oligophosphates (NpnN, n>5), a group of cellular signaling molecules. At optimal pH 8.5, the enzyme actively degrades adenosine (5')-pentaphospho-(5')-adenosine (Ap5A) into ATP and ADP with a Km of 0.1 mM and kcat of 1.9 s-1. Guanosine (5')-pentaphospho-(5')-guanosine (Gp5G) as well as adenosine-(5')- hexaphospho (5')-adenosine (Ap6A) are also substrates. Similar to other Nudix hydrolases, InvA requires a divalent metal cation, Mg2+ or Zn2+ for optimal activity. These data suggest that the rickettsial invasion protein likely plays a role in controlling the concentration of stress-induced dinucleoside oligophosphates following bacterial invasion.


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