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Journal of Bacteriology, June 2009, p. 3629-3638, Vol. 191, No. 11
0021-9193/09/$08.00+0     doi:10.1128/JB.00811-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Sialic Acid (N-Acetyl Neuraminic Acid) Utilization by Bacteroides fragilis Requires a Novel N-Acetyl Mannosamine Epimerase{triangledown} ,{dagger}

Christopher Brigham,{ddagger} Ruth Caughlan,§ Rene Gallegos, Mary Beth Dallas,|| Veronica G. Godoy,# and Michael H. Malamy*

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111

Received 9 June 2008/ Accepted 17 March 2009

We characterized the nanLET operon in Bacteroides fragilis, whose products are required for the utilization of the sialic acid N-acetyl neuraminic acid (NANA) as a carbon and energy source. The first gene of the operon is nanL, which codes for an aldolase that cleaves NANA into N-acetyl mannosamine (manNAc) and pyruvate. The next gene, nanE, codes for a manNAc/N-acetylglucosamine (NAG) epimerase, which, intriguingly, possesses more similarity to eukaryotic renin binding proteins than to other bacterial NanE epimerase proteins. Unphosphorylated manNAc is the substrate of NanE, while ATP is a cofactor in the epimerase reaction. The third gene of the operon is nanT, which shows similarity to the major transporter facilitator superfamily and is most likely to be a NANA transporter. Deletion of any of these genes eliminates the ability of B. fragilis to grow on NANA. Although B. fragilis does not normally grow with manNAc as the sole carbon source, we isolated a B. fragilis mutant strain that can grow on this substrate, likely due to a mutation in a NAG transporter; both manNAc transport and NAG transport are affected in this strain. Deletion of the nanE epimerase gene or the rokA hexokinase gene, whose product phosphorylates NAG, in the manNAc-enabled strain abolishes growth on manNAc. Thus, B. fragilis possesses a new pathway of NANA utilization, which we show is also found in other Bacteroides species.

* Corresponding author. Mailing address: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. Phone: (617) 636-6756. Fax: (617) 636-0337. E-mail: michael.malamy{at}tufts.edu

{triangledown} Published ahead of print on 20 March 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

{ddagger} Present address: Department of Biology, MIT, Cambridge, MA 02139.

§ Present address: Infectious Diseases, Novartis Institute for Biomedical Research, Cambridge, MA 02139.

|| Present address: Department of Structural and Molecular Biochemistry, North Carolina State University, Raleigh, NC 27695.

# Present address: Department of Biology, Northeastern University, Boston, MA 02115.

Journal of Bacteriology, June 2009, p. 3629-3638, Vol. 191, No. 11
0021-9193/09/$08.00+0     doi:10.1128/JB.00811-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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