Differential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat

Chi-Hung Lin, Robyn A. Peterson, Audrey Gueniche, Ségolène Adam de Beaumais, Virginie Hourblin, Lionel Breton, Maria Dalko, Nicolle H. Packer

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Sweat is a secretory fluid that can be a source of unpleasant body odour due to interaction of resident bacteria with sweat components. Identification of glycoproteins in sweat suggests that protein-conjugated glycans may act as binding epitopes for bacteria, as found in other secretory fluids such as human milk, tears and saliva which help to protect epithelial surfaces from infection.

We conducted proteomic and glycomic analysis of sweat to reveal an abundance of glycoproteins, predominantly carrying bi-antennary sialylated N-glycans with or without fucose. A fluorescent plate assay was used to determine whether glycans on sweat proteins provide binding epitopes for odour-producing skin commensals Staphylococcus epidermidis and Corynebacterium. Sialic acid and fucose were found to be important binding epitopes for S. epidermidis 3-22-BD-6, a strain recently isolated from human sweat, whereas fucose (but not sialic acid) contributed to the binding of Type strain S. epidermidis ATCC 12228. In contrast, our results indicate that sweat N-glycans do not provide binding epitopes for Corynebacterium.

Synthetic sugar mimics of Lewis blood group antigens were investigated as potential inhibitors of the binding of S. epidermidis 3-22-BD-6 to sweat. Pre-incubation of the bacterium with LeB, LeX, LeY and sLeX (pentaose) resulted in a significant reduction in sweat protein adhesion indicating that terminal fucose is a key binding epitope, particularly when linked to a Type 2 chain (Galβ1-4GlcNAc) configuration (LeY).

Our results form an impetus for future studies seeking to elucidate the role of glycans in sweat associated malodour, with possible implications for cosmetic and medical fields.

LanguageEnglish
Pages53-60
Number of pages8
JournalMicrobiological Research
Volume220
DOIs
Publication statusPublished - Mar 2019

Fingerprint

Corynebacterium
Staphylococcus epidermidis
Sweat
Polysaccharides
Fucose
Epitopes
N-Acetylneuraminic Acid
Bacteria
Glycoproteins
Glycomics
Human Milk
Blood Group Antigens
Tears
Saliva
Protein Binding
Cosmetics
Proteomics
Proteins

Keywords

  • Sweat
  • Glycan
  • Glycoprotein
  • Fucose
  • Staphylococcus
  • Corynebacterium

Cite this

Lin, Chi-Hung ; Peterson, Robyn A. ; Gueniche, Audrey ; de Beaumais, Ségolène Adam ; Hourblin, Virginie ; Breton, Lionel ; Dalko, Maria ; Packer, Nicolle H. / Differential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat. In: Microbiological Research. 2019 ; Vol. 220. pp. 53-60.
@article{a64f0c690df84d07a5ab6320c8ff3190,
title = "Differential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat",
abstract = "Sweat is a secretory fluid that can be a source of unpleasant body odour due to interaction of resident bacteria with sweat components. Identification of glycoproteins in sweat suggests that protein-conjugated glycans may act as binding epitopes for bacteria, as found in other secretory fluids such as human milk, tears and saliva which help to protect epithelial surfaces from infection. We conducted proteomic and glycomic analysis of sweat to reveal an abundance of glycoproteins, predominantly carrying bi-antennary sialylated N-glycans with or without fucose. A fluorescent plate assay was used to determine whether glycans on sweat proteins provide binding epitopes for odour-producing skin commensals Staphylococcus epidermidis and Corynebacterium. Sialic acid and fucose were found to be important binding epitopes for S. epidermidis 3-22-BD-6, a strain recently isolated from human sweat, whereas fucose (but not sialic acid) contributed to the binding of Type strain S. epidermidis ATCC 12228. In contrast, our results indicate that sweat N-glycans do not provide binding epitopes for Corynebacterium. Synthetic sugar mimics of Lewis blood group antigens were investigated as potential inhibitors of the binding of S. epidermidis 3-22-BD-6 to sweat. Pre-incubation of the bacterium with LeB, LeX, LeY and sLeX (pentaose) resulted in a significant reduction in sweat protein adhesion indicating that terminal fucose is a key binding epitope, particularly when linked to a Type 2 chain (Galβ1-4GlcNAc) configuration (LeY). Our results form an impetus for future studies seeking to elucidate the role of glycans in sweat associated malodour, with possible implications for cosmetic and medical fields.",
keywords = "Sweat, Glycan, Glycoprotein, Fucose, Staphylococcus, Corynebacterium",
author = "Chi-Hung Lin and Peterson, {Robyn A.} and Audrey Gueniche and {de Beaumais}, {S{\'e}gol{\`e}ne Adam} and Virginie Hourblin and Lionel Breton and Maria Dalko and Packer, {Nicolle H.}",
year = "2019",
month = "3",
doi = "10.1016/j.micres.2018.12.007",
language = "English",
volume = "220",
pages = "53--60",
journal = "Microbiological Research",
issn = "0944-5013",
publisher = "Urban und Fischer Verlag Jena",

}

Differential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat. / Lin, Chi-Hung; Peterson, Robyn A.; Gueniche, Audrey; de Beaumais, Ségolène Adam; Hourblin, Virginie; Breton, Lionel; Dalko, Maria; Packer, Nicolle H.

In: Microbiological Research, Vol. 220, 03.2019, p. 53-60.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Differential involvement of glycans in the binding of Staphylococcus epidermidis and Corynebacterium spp. to human sweat

AU - Lin, Chi-Hung

AU - Peterson, Robyn A.

AU - Gueniche, Audrey

AU - de Beaumais, Ségolène Adam

AU - Hourblin, Virginie

AU - Breton, Lionel

AU - Dalko, Maria

AU - Packer, Nicolle H.

PY - 2019/3

Y1 - 2019/3

N2 - Sweat is a secretory fluid that can be a source of unpleasant body odour due to interaction of resident bacteria with sweat components. Identification of glycoproteins in sweat suggests that protein-conjugated glycans may act as binding epitopes for bacteria, as found in other secretory fluids such as human milk, tears and saliva which help to protect epithelial surfaces from infection. We conducted proteomic and glycomic analysis of sweat to reveal an abundance of glycoproteins, predominantly carrying bi-antennary sialylated N-glycans with or without fucose. A fluorescent plate assay was used to determine whether glycans on sweat proteins provide binding epitopes for odour-producing skin commensals Staphylococcus epidermidis and Corynebacterium. Sialic acid and fucose were found to be important binding epitopes for S. epidermidis 3-22-BD-6, a strain recently isolated from human sweat, whereas fucose (but not sialic acid) contributed to the binding of Type strain S. epidermidis ATCC 12228. In contrast, our results indicate that sweat N-glycans do not provide binding epitopes for Corynebacterium. Synthetic sugar mimics of Lewis blood group antigens were investigated as potential inhibitors of the binding of S. epidermidis 3-22-BD-6 to sweat. Pre-incubation of the bacterium with LeB, LeX, LeY and sLeX (pentaose) resulted in a significant reduction in sweat protein adhesion indicating that terminal fucose is a key binding epitope, particularly when linked to a Type 2 chain (Galβ1-4GlcNAc) configuration (LeY). Our results form an impetus for future studies seeking to elucidate the role of glycans in sweat associated malodour, with possible implications for cosmetic and medical fields.

AB - Sweat is a secretory fluid that can be a source of unpleasant body odour due to interaction of resident bacteria with sweat components. Identification of glycoproteins in sweat suggests that protein-conjugated glycans may act as binding epitopes for bacteria, as found in other secretory fluids such as human milk, tears and saliva which help to protect epithelial surfaces from infection. We conducted proteomic and glycomic analysis of sweat to reveal an abundance of glycoproteins, predominantly carrying bi-antennary sialylated N-glycans with or without fucose. A fluorescent plate assay was used to determine whether glycans on sweat proteins provide binding epitopes for odour-producing skin commensals Staphylococcus epidermidis and Corynebacterium. Sialic acid and fucose were found to be important binding epitopes for S. epidermidis 3-22-BD-6, a strain recently isolated from human sweat, whereas fucose (but not sialic acid) contributed to the binding of Type strain S. epidermidis ATCC 12228. In contrast, our results indicate that sweat N-glycans do not provide binding epitopes for Corynebacterium. Synthetic sugar mimics of Lewis blood group antigens were investigated as potential inhibitors of the binding of S. epidermidis 3-22-BD-6 to sweat. Pre-incubation of the bacterium with LeB, LeX, LeY and sLeX (pentaose) resulted in a significant reduction in sweat protein adhesion indicating that terminal fucose is a key binding epitope, particularly when linked to a Type 2 chain (Galβ1-4GlcNAc) configuration (LeY). Our results form an impetus for future studies seeking to elucidate the role of glycans in sweat associated malodour, with possible implications for cosmetic and medical fields.

KW - Sweat

KW - Glycan

KW - Glycoprotein

KW - Fucose

KW - Staphylococcus

KW - Corynebacterium

UR - http://www.scopus.com/inward/record.url?scp=85059471367&partnerID=8YFLogxK

U2 - 10.1016/j.micres.2018.12.007

DO - 10.1016/j.micres.2018.12.007

M3 - Article

VL - 220

SP - 53

EP - 60

JO - Microbiological Research

T2 - Microbiological Research

JF - Microbiological Research

SN - 0944-5013

ER -