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Infection and Immunity, November 2005, p. 7390-7397, Vol. 73, No. 11
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.11.7390-7397.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Enhanced Factor H Binding to Sialylated Gonococci Is Restricted to the Sialylated Lacto-N-Neotetraose Lipooligosaccharide Species: Implications for Serum Resistance and Evidence for a Bifunctional Lipooligosaccharide Sialyltransferase in Gonococci

Sunita Gulati,1 Andrew Cox,2 Lisa A. Lewis,3 Frank St. Michael,2 Jianjun Li,2 Ryan Boden,3 Sanjay Ram,3* and Peter A. Rice1

Division of Infectious Diseases and Immunology, University of Massachusetts Medical School, Worcester, Massachusetts 01605,1 National Research Council, Ottawa, ON K1A 0R6, Canada,2 Evans Biomedical Research Center, Boston University Medical Center, Boston, Massachusetts 021183

Received 25 February 2005/ Returned for modification 13 April 2005/ Accepted 5 August 2005

We isolated serologically identical (by serovar determination and porin variable region [VR] typing) strains of Neisseria gonorrhoeae from an infected male and two of his monogamous female sex partners. One strain (termed 398078) expressed the L1 (Gal{alpha}1 -> 3Galß1 -> 4Glcß1 -> 4HepI) lipooligosaccharide (LOS) structure exclusively; the other (termed 398079) expressed the lacto-N-neotetraose (LNT; Galß1 -> 4GlcNAcß1 -> 3Galß1 -> 4Glcß1 -> 4HepI) LOS structure. The strain from the male index case expressed both glycoforms and exhibited both immunotypes. Nuclear magnetic resonance analysis revealed that sialic acid linked to the terminal Gal of L1 LOS via an {alpha}2 -> 6 linkage and, as expected, to the terminal Gal of LNT LOS via an {alpha}2-> 3 linkage. Insertional inactivation of the sialyltransferase gene (known to sialylate LNT LOS) abrogated both L1 LOS sialylation and LNT LOS sialylation, suggesting a bifunctional nature of this enzyme in gonococci. Akin to our previous observations, sialylation of the LNT LOS of strain 398079 enhanced the binding of the complement regulatory molecule, factor H. Rather surprisingly, factor H did not bind to sialylated strain 398078. LOS sialylation conferred the LNT LOS-bearing strain complete (100%) resistance to killing by even 50% nonimmune normal human serum (NHS), whereas sialylation of L1 LOS conferred resistance only to 10% NHS. The ability of gonococcal sialylated LNT to bind factor H confers high-level serum resistance, which is not seen with sialylated L1 LOS. Thus, serum resistance mediated by sialylation of gonococcal L1 and LNT LOS occurs by different mechanisms, and specificity of factor H binding to sialylated gonococci is restricted to the LNT LOS species.

* Corresponding author. Mailing address: Section of Infectious Diseases, Evans Biomedical Research Center, Boston University Medical Center, Room 627, 650 Albany Street, Boston, MA 02118. Phone: (617) 414-7917. Fax: (617) 414-5280. E-mail: sram{at}bu.edu.

Editor: J. N. Weiser

Infection and Immunity, November 2005, p. 7390-7397, Vol. 73, No. 11
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.11.7390-7397.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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