A Novel Sialylation Site on Neisseria gonorrhoeae Lipooligosaccharide Links Heptose II Lactose Expression with Pathogenicity

Author:

Ram Sanjay1,Gulati Sunita1,Lewis Lisa A.1,Chakraborti Srinjoy1,Zheng Bo1,DeOliveira Rosane B.1,Reed George W.2,Cox Andrew D.3,Li Jianjun3,St. Michael Frank3,Stupak Jacek3,Su Xiao-Hong4,Saha Sudeshna56,Landig Corinna S.56,Varki Ajit56,Rice Peter A.1

Affiliation:

1. Division of Infectious Diseases and Immunology, University of Massachusetts Medical School, Worcester, Massachusetts, USA

2. Preventive and Behavioral Medicine, University of Massachusetts Medical School, Worcester, Massachusetts, USA

3. Human Health Therapeutics Portfolio, National Research Council of Canada, Ottawa, Ontario, Canada

4. Department of STD, Institute of Dermatology, Chinese Academy of Medical Sciences and Peking Union Medical College, Nanjing, People's Republic of China

5. Department of Medicine and Cellular and Molecular Medicine, University of California, San Diego, La Jolla, California, USA

6. Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA

Abstract

Sialylation of lacto- N -neotetraose (LNnT) extending from heptose I (HepI) of gonococcal lipooligosaccharide (LOS) contributes to pathogenesis. Previously, gonococcal LOS sialyltransterase (Lst) was shown to sialylate LOS in Triton X-100 extracts of strain 15253, which expresses lactose from both HepI and HepII, the minimal structure required for monoclonal antibody (MAb) 2C7 binding.

Funder

HHS | National Institutes of Health

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

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