Title

Molecular Characterization Of The Borrelia Burgdorferi In Vivo-Essential Protein Pnca

Abstract

The conversion of nicotinamide to nicotinic acid by nicotinamidase enzymes is a critical step in maintaining NAD + homeostasis and contributes to numerous important biological processes in diverse organisms. In Borrelia burgdorferi, the nicotinamidase enzyme, PncA, is required for spirochaete survival throughout the infectious cycle. Mammals lack nicotinamidases and therefore PncA may serve as a therapeutic target for Lyme disease. Contrary to the in vivo importance of PncA, the current annotation for the pncA ORF suggests that the encoded protein may be inactive due to the absence of an N-terminal aspartic acid residue that is a conserved member of the catalytic triad of characterized PncA proteins. Herein, we have used genetic and biochemical strategies to determine the N-terminal sequence of B. burgdorferi PncA. Our data demonstrate that the PncA protein is 24 aa longer than the currently annotated sequence and that pncA translation is initiated from the rare, non-canonical initiation codon AUU. These findings are an important first step in understanding the catalytic function of this in vivo-essential protein. © 2011 SGM.

Publication Date

10-1-2011

Publication Title

Microbiology

Volume

157

Issue

10

Number of Pages

2831-2840

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1099/mic.0.051706-0

Socpus ID

80053459870 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/80053459870

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