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J. Biol. Chem., Vol. 279, Issue 41, 42765-42773, October 8, 2004

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The Neisseria meningitidis Serogroup A Capsular Polysaccharide O-3 and O-4 Acetyltransferase^*

Seshu K. Gudlavalleti, Anup K. Datta, Yih-Ling Tzeng, Corie Noble¶, Russell W. Carlson, and David S. Stephens¶||**

From the Departments of Medicine and ^||Microbiology and Immunology, Division of Infectious Diseases, Emory University School of Medicine, Atlanta, Georgia 30322, the ^¶Department of Veterans Affairs, Atlanta, Georgia 30033, and the Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602

Neisseria meningitidis serogroup A capsular polysaccharide (CPS) is composed of a homopolymer of O-acetylated, 16-linked ManNAc 1-phosphate that is distinct from the capsule structures of the other meningococcal disease-causing serogroups, B, C, Y, and W-135. The serogroup A capsule biosynthetic genetic cassette consists of four open reading frames, mynA–D (sacA–D), that are specific to serogroup A, but the functions of these genes have not been well characterized. mynC was found to encode an inner membrane-associated acetyltransferase that is responsible for the O-acetylation of the CPS of serogroup A. The wild-type CPS as revealed by ¹H NMR had 60–70% O-acetylated ManNAc residues that contained acetyl groups at O-3, with some species acetylated at O-4 and at both O-3 and O-4. A non-polar mynC mutant generated by introducing an aphA-3 kanamycin resistance cassette produced CPS with no O-acetylation. A serogroup A capsule-specific monoclonal antibody was shown to recognize the wild-type O-acetylated CPS, but not the CPS of the mynC mutant, which lacked O-acetylation. MynC was C-terminally His-tagged and overexpressed in Escherichia coli to obtain the predicted 26-kDa protein. The acetyltransferase activity of purified MynC was demonstrated in vitro using [¹⁴C]acetyl-CoA. MynC O-acetylated the O-acetylated CPS of the mynC mutant and further acetylated the wild-type CPS of serogroup A meningococci, but not the CPS of serogroup B or C meningococci. Genetic complementation of the mynC mutant confirmed the function of MynC as the serogroup A CPS O-3 and O-4 acetyltransferase. MynC represents a new subclass of O-acetyltransferases that utilize acetyl-CoA to decorate the D-mannosamine capsule of N. meningitidis serogroup A.

Received for publication, December 10, 2003 , and in revised form, August 3, 2004.

^* This work was supported by United States Public Health Service Grant AI40247 from the National Institutes of Health (to D. S. S.). The structural analytical work was supported in part by Department of Energy Grant DE-FG02-93ER20097 (to the Complex Carbohydrate Research Center, University of Georgia). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence should be addressed: Research Service (151-I), Dept. of Veterans Affairs, 1670 Clairmont Rd., Decatur, GA 30033. Tel.: 404-728-7688; Fax: 404-329-2210; E-mail: dstep01{at}emory.edu.

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