Human α-amylase present in lower-genital-tract mucosal fluid processes glycogen to support vaginal colonization by Lactobacillus

Gregory T. Spear, Audrey L. French, Douglas Gilbert, M. Reza Zariffard, Paria Mirmonsef, Thomas H. Sullivan, William W. Spear, Alan Landay, Sandra Micci, Byung Hoo Lee, Bruce R. Hamaker

Research output: Contribution to journalArticlepeer-review

158 Scopus citations

Abstract

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 α-amylase. A temperature-dependent glycogen-degrading activity was detected in genital fluids that correlated with levels of α-amylase. Treatment of glycogen with genital fluids resulted in production of maltose, maltotriose, and maltotetraose, the major products of α-amylase digestion. These studies show that human α-amylase is present in the female lower genital tract and elucidates how epithelial glycogen can support Lactobacillus colonization in the genital tract.

Original languageEnglish (US)
Pages (from-to)1019-1028
Number of pages10
JournalJournal of Infectious Diseases
Volume210
Issue number7
DOIs
StatePublished - Oct 1 2014
Externally publishedYes

Keywords

  • Female genital tract
  • Glycogen
  • Lactobacillus
  • Maltose
  • α-amylase

ASJC Scopus subject areas

  • General Medicine

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