Review

Mucinases and sialidases: their role in the pathogenesis of sexually transmitted infections in the female genital tract

R Wiggins¹, S J Hicks², P W Soothill³, M R Millar⁴ and A P Corfield¹

¹ Dorothy Crowfoot Hodgkin Laboratories, University Division of Medicine, Bristol Royal Infirmary, Bristol BS2 8HW, UK
² Centre for Biomedical Sciences, School of Applied Sciences, University of Wales Institute Cardiff Western Ave, Cardiff CF5 2YB, UK
³ University Department of Obstetrics and Gynaecology, St Michael's Hospital, Southwell Street, Bristol BS2 8EG, UK
⁴ Department of Microbiology, Bart's and the London NHS Trust, Smithfield, London EC1A 7BE, UK

Correspondence to:
Dr A P Corfield tony.corfield{at}bristol.ac.uk

Background: Mucinases and sialidases contribute to the process of invasion and colonisation in many conditions and infections of the female reproductive tract by degrading the protective cervical mucus. The role of hydrolytic enzymes in the pathogenesis of sexually transmitted diseases and their effect on cervical mucus are discussed in this review.

Methods: Articles were searched for using the keywords "sialidase," "mucinase," "protease," and "sexually transmitted infections." As well as review and other articles held by our group, searches were conducted using PubMed, Grateful Med, and the University of Bath search engine, BIDS.

Results: Numerous publications were found describing the production of hydrolytic enzymes in sexually transmitted diseases. Because the number of publications exceeded the restrictions imposed on the size of the review, the authors selected and discussed those which they considered of the most relevance to sexually transmitted infections.

Key Words: mucinase; sialidase; microbial protease

Abbreviations: BSM (bovine submaxillary mucin), BV (bacterial vaginosis); Fuc (fucose); Gal (galactose); GalNAc (N-acetylgalactosamine); Glc (glucose); GlcNAc (N-acetylglucosamine); Man (mannose); PMN (polymorphonuclear neutrophils), human immunodeficiency virus 1 (HIV-1); sIgA (secretory immunoglobulin A).

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