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 odourproducing 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.

In vitro model of human mammary gland microbial colonization (MAGIC) demonstrates distinctive cytokine response to imbalanced human milk microbiota

“…For example, the adhesion rate of S. epidermidis was much higher compared with Corynebacterium tuberculostearicum . Microorganisms differ in their adhesion mechanisms and often show a preference for certain host glycan moieties according to the specific affinities of microbial glycan-binding proteins or lectins on the cell surface ( 33 ). The fact that Corynebacterium species differ greatly in their ability to adhere to different mucus glycans ( 33 , 34 ) may provide an explanation for the lower adherence of Corynebacterium .…”

“…Microorganisms differ in their adhesion mechanisms and often show a preference for certain host glycan moieties according to the specific affinities of microbial glycan-binding proteins or lectins on the cell surface ( 33 ). The fact that Corynebacterium species differ greatly in their ability to adhere to different mucus glycans ( 33 , 34 ) may provide an explanation for the lower adherence of Corynebacterium . SEM micrographs showed that not only live bacteria but also dead or damaged bacteria can adhere and interact with the epithelium ( Fig.…”

Monitoring Salivary Sialic Acid and Sialidase Activity to Assess Oral Health Status: Results of a Single Site Double-Blind Study

“…In addition to the above, a possible avenue for future research direction is from a recent investigation that reports sialic acid in other body fluids such as sweat. Results from that investigation examined the binding of skin bacteria to these ligands with the intent of identifying future therapeutic mechanisms to mitigate the effects of skin bacteria [34].…”

Detailed Characterization of Antipathogenic Properties of Human Milk N-Glycome, against Staphylococcus aureus, Indicating Its Targeting on Cell Surface Proteins

“…The binding assay was a modified version of a previous method. , The detailed procedure can be found in the Supporting Information.…”