Amylases in the Human Vagina
ABSTRACT Dominance of Lactobacillus species in vaginal communities is a hallmark of healthy conditions in the female genital tract. Key nutrients for lactobacilli include sugars produced when glycogen is degraded by α-amylase in the vagina. While α-amylase activity has been demonstrated in vaginal f...
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American Society for Microbiology
2020
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oai:doaj.org-article:3b5d874276874c7da41fe15f02b75a822021-11-15T15:31:13ZAmylases in the Human Vagina10.1128/mSphere.00943-202379-5042https://doaj.org/article/3b5d874276874c7da41fe15f02b75a822020-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00943-20https://doaj.org/toc/2379-5042ABSTRACT Dominance of Lactobacillus species in vaginal communities is a hallmark of healthy conditions in the female genital tract. Key nutrients for lactobacilli include sugars produced when glycogen is degraded by α-amylase in the vagina. While α-amylase activity has been demonstrated in vaginal fluids, it is unclear whether α-amylases are produced solely by the host, bacteria in the vagina, or both. We screened cervicovaginal mucus from 23 reproductive-age women, characterized the species composition of vaginal communities, measured vaginal pH, and determined levels of amylase activity, glycogen, and lactic acid. Based on differences in these measured variables, one sample from each of four individual donors was selected for metagenomic and proteomic analyses. Of eight putative bacterial amylases identified in the assembled bacterial metagenomes, we detected four in vaginal fluids. These amylases were produced by various bacteria in different vaginal communities. Moreover, no two communities were the same in terms of which bacteria were producing amylases. Although we detected bacterial amylases in vaginal fluids, there was no clear association between the bacterial species that was dominant in a community and the level of amylase activity. This association was likely masked by the presence of human α-amylase, which was also detected in vaginal fluids. Finally, the levels of amylase activity and glycogen were only weakly associated. Our findings show, for the first time, that multiple amylases from both bacterial and human origins can be present simultaneously in the vagina. This work also suggests that the link between glycogen, amylase, and Lactobacillus in the vagina is complex. IMPORTANCE In this study, we show that multiple bacteria in the vaginal community produce amylases that hydrolyze glycogen into simpler sugars (i.e., maltose and maltotriose). These sugars serve as “common goods” that sustain bacterial populations in vaginal communities. Given the temporal changes that are observed in the human vaginal microbiome, we expect the kinds of bacterial amylases produced will also vary over time. These differences influence the pool of resources that are broadly shared and shape the species composition of the vaginal bacterial community.Kenetta L. NunnGeremy C. ClairJoshua N. AdkinsKristin EngbrechtThomas FillmoreLarry J. ForneyAmerican Society for MicrobiologyarticleamylaseglycogenLactobacillusvaginal microbiomeMicrobiologyQR1-502ENmSphere, Vol 5, Iss 6 (2020) |
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amylase glycogen Lactobacillus vaginal microbiome Microbiology QR1-502 |
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amylase glycogen Lactobacillus vaginal microbiome Microbiology QR1-502 Kenetta L. Nunn Geremy C. Clair Joshua N. Adkins Kristin Engbrecht Thomas Fillmore Larry J. Forney Amylases in the Human Vagina |
description |
ABSTRACT Dominance of Lactobacillus species in vaginal communities is a hallmark of healthy conditions in the female genital tract. Key nutrients for lactobacilli include sugars produced when glycogen is degraded by α-amylase in the vagina. While α-amylase activity has been demonstrated in vaginal fluids, it is unclear whether α-amylases are produced solely by the host, bacteria in the vagina, or both. We screened cervicovaginal mucus from 23 reproductive-age women, characterized the species composition of vaginal communities, measured vaginal pH, and determined levels of amylase activity, glycogen, and lactic acid. Based on differences in these measured variables, one sample from each of four individual donors was selected for metagenomic and proteomic analyses. Of eight putative bacterial amylases identified in the assembled bacterial metagenomes, we detected four in vaginal fluids. These amylases were produced by various bacteria in different vaginal communities. Moreover, no two communities were the same in terms of which bacteria were producing amylases. Although we detected bacterial amylases in vaginal fluids, there was no clear association between the bacterial species that was dominant in a community and the level of amylase activity. This association was likely masked by the presence of human α-amylase, which was also detected in vaginal fluids. Finally, the levels of amylase activity and glycogen were only weakly associated. Our findings show, for the first time, that multiple amylases from both bacterial and human origins can be present simultaneously in the vagina. This work also suggests that the link between glycogen, amylase, and Lactobacillus in the vagina is complex. IMPORTANCE In this study, we show that multiple bacteria in the vaginal community produce amylases that hydrolyze glycogen into simpler sugars (i.e., maltose and maltotriose). These sugars serve as “common goods” that sustain bacterial populations in vaginal communities. Given the temporal changes that are observed in the human vaginal microbiome, we expect the kinds of bacterial amylases produced will also vary over time. These differences influence the pool of resources that are broadly shared and shape the species composition of the vaginal bacterial community. |
format |
article |
author |
Kenetta L. Nunn Geremy C. Clair Joshua N. Adkins Kristin Engbrecht Thomas Fillmore Larry J. Forney |
author_facet |
Kenetta L. Nunn Geremy C. Clair Joshua N. Adkins Kristin Engbrecht Thomas Fillmore Larry J. Forney |
author_sort |
Kenetta L. Nunn |
title |
Amylases in the Human Vagina |
title_short |
Amylases in the Human Vagina |
title_full |
Amylases in the Human Vagina |
title_fullStr |
Amylases in the Human Vagina |
title_full_unstemmed |
Amylases in the Human Vagina |
title_sort |
amylases in the human vagina |
publisher |
American Society for Microbiology |
publishDate |
2020 |
url |
https://doaj.org/article/3b5d874276874c7da41fe15f02b75a82 |
work_keys_str_mv |
AT kenettalnunn amylasesinthehumanvagina AT geremycclair amylasesinthehumanvagina AT joshuanadkins amylasesinthehumanvagina AT kristinengbrecht amylasesinthehumanvagina AT thomasfillmore amylasesinthehumanvagina AT larryjforney amylasesinthehumanvagina |
_version_ |
1718427819683348480 |