4.7 Article

Human α-amylase Present in Lower-Genital-Tract Mucosal Fluid Processes Glycogen to Support Vaginal Colonization by Lactobacillus

Journal

JOURNAL OF INFECTIOUS DISEASES
Volume 210, Issue 7, Pages 1019-1028

Publisher

OXFORD UNIV PRESS INC
DOI: 10.1093/infdis/jiu231

Keywords

alpha-amylase; female genital tract; glycogen; Lactobacillus; maltose

Funding

  1. National Institutes of Health (NIH) [P01 AI08297, P30 AI 082151]

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Lactobacillus colonization of the lower female genital tract provides protection from the acquisition of sexually transmitted diseases, including human immunodeficiency virus, and from adverse pregnancy outcomes. While glycogen in vaginal epithelium is thought to support Lactobacillus colonization in vivo, many Lactobacillus isolates cannot utilize glycogen in vitro. This study investigated how glycogen could be utilized by vaginal lactobacilli in the genital tract. Several Lactobacillus isolates were confirmed to not grow in glycogen, but did grow in glycogen-breakdown products, including maltose, maltotriose, maltopentaose, maltodextrins, and glycogen treated with salivary alpha-amylase. A temperature-dependent glycogen-degrading activity was detected in genital fluids that correlated with levels of alpha-amylase. Treatment of glycogen with genital fluids resulted in production of maltose, maltotriose, and maltotetraose, the major products of alpha-amylase digestion. These studies show that human alpha-amylase is present in the female lower genital tract and elucidates how epithelial glycogen can support Lactobacillus colonization in the genital tract.

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