Glycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap

ABSTRACT Staphylococcus epidermidis and other coagulase-negative staphylococci (CoNS) that colonize skin are known to promote skin immunity and inhibit colonization of pathogens that cause skin and soft tissue infections, including Staphylococcus aureus. However, S. epidermidis adherence to corneocy...

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Autores principales:	Paroma Roy, Alexander R. Horswill, Paul D. Fey
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2021
Materias:	accumulation-associated protein Staphylococcus aureus Staphylococcus epidermidis skin adherence Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/a7639c5ecae24c0b998eb452d0f159b1
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spelling	oai:doaj.org-article:a7639c5ecae24c0b998eb452d0f159b12021-11-10T18:37:52ZGlycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap10.1128/mBio.02908-202150-7511https://doaj.org/article/a7639c5ecae24c0b998eb452d0f159b12021-08-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.02908-20https://doaj.org/toc/2150-7511ABSTRACT Staphylococcus epidermidis and other coagulase-negative staphylococci (CoNS) that colonize skin are known to promote skin immunity and inhibit colonization of pathogens that cause skin and soft tissue infections, including Staphylococcus aureus. However, S. epidermidis adherence to corneocytes, the cells that constitute the uppermost layer of the skin epidermis, remains poorly understood. Our study documents that S. epidermidis corneocyte adherence is dependent upon the accumulation-associated protein (Aap). Aap is composed of two distinct A and B domains. The A domain is comprised of a repeat region and a conserved L-type lectin domain, whereas the fibrillar B domain, which is comprised of G5 and E repeats, is linked to the cell wall in a sortase-dependent manner. Our studies revealed that adherence to corneocytes is dependent upon the lectin subdomain within the A domain. However, significant adherence was only observed when the lectin domain was expressed with both the A repeat and the B domain, suggesting further interactions between these three domains. Our data also suggest that the A repeat domain is important for stability or expression of Aap. Deglycosylation treatment suggested that glycans expressed in the host stratum corneum serve as potential binding partners for Aap-mediated corneocyte adherence. Last, bioinformatic analyses of the predominant commensal species of CoNS identified open reading frames (ORFs) homologous to aap, thus suggesting that Aap orthologues containing lectin-like domains may provide the basis for staphylococcal colonization of skin. Corroborating these observations, adherence to corneocytes in an S. aureus mgrA mutant was dependent upon SasG, the Aap orthologue in S. aureus. IMPORTANCE Staphylococcus aureus is the most significant cause of skin and soft tissue infections yet it rarely colonizes the skin of healthy individuals. This is believed to be due, in part, to inhibition of colonization via toxic substances produced by normal skin flora, including by S. epidermidis. Furthermore, we surmise that S. aureus colonization inhibition may also be due to competition for binding sites on host corneocytes. To understand these potential interactions between S. aureus and S. epidermidis and, potentially, other coagulase-negative staphylococci, we must first understand how staphylococci adhere to corneocytes. This work documents that S. epidermidis adherence to corneocytes is dependent upon the fibrillar cell wall-associated protein Aap. Our work further documents that Aap binds to glycans exposed on the corneocyte surface, which are commonly exploited by bacteria to facilitate adherence to host cells. Furthermore, we find that Aap orthologues may be responsible for corneocyte adherence in other staphylococci, including in S. aureus.Paroma RoyAlexander R. HorswillPaul D. FeyAmerican Society for Microbiologyarticleaccumulation-associated proteinStaphylococcus aureusStaphylococcus epidermidisskin adherenceMicrobiologyQR1-502ENmBio, Vol 12, Iss 4 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	accumulation-associated protein Staphylococcus aureus Staphylococcus epidermidis skin adherence Microbiology QR1-502
spellingShingle	accumulation-associated protein Staphylococcus aureus Staphylococcus epidermidis skin adherence Microbiology QR1-502 Paroma Roy Alexander R. Horswill Paul D. Fey Glycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap
description	ABSTRACT Staphylococcus epidermidis and other coagulase-negative staphylococci (CoNS) that colonize skin are known to promote skin immunity and inhibit colonization of pathogens that cause skin and soft tissue infections, including Staphylococcus aureus. However, S. epidermidis adherence to corneocytes, the cells that constitute the uppermost layer of the skin epidermis, remains poorly understood. Our study documents that S. epidermidis corneocyte adherence is dependent upon the accumulation-associated protein (Aap). Aap is composed of two distinct A and B domains. The A domain is comprised of a repeat region and a conserved L-type lectin domain, whereas the fibrillar B domain, which is comprised of G5 and E repeats, is linked to the cell wall in a sortase-dependent manner. Our studies revealed that adherence to corneocytes is dependent upon the lectin subdomain within the A domain. However, significant adherence was only observed when the lectin domain was expressed with both the A repeat and the B domain, suggesting further interactions between these three domains. Our data also suggest that the A repeat domain is important for stability or expression of Aap. Deglycosylation treatment suggested that glycans expressed in the host stratum corneum serve as potential binding partners for Aap-mediated corneocyte adherence. Last, bioinformatic analyses of the predominant commensal species of CoNS identified open reading frames (ORFs) homologous to aap, thus suggesting that Aap orthologues containing lectin-like domains may provide the basis for staphylococcal colonization of skin. Corroborating these observations, adherence to corneocytes in an S. aureus mgrA mutant was dependent upon SasG, the Aap orthologue in S. aureus. IMPORTANCE Staphylococcus aureus is the most significant cause of skin and soft tissue infections yet it rarely colonizes the skin of healthy individuals. This is believed to be due, in part, to inhibition of colonization via toxic substances produced by normal skin flora, including by S. epidermidis. Furthermore, we surmise that S. aureus colonization inhibition may also be due to competition for binding sites on host corneocytes. To understand these potential interactions between S. aureus and S. epidermidis and, potentially, other coagulase-negative staphylococci, we must first understand how staphylococci adhere to corneocytes. This work documents that S. epidermidis adherence to corneocytes is dependent upon the fibrillar cell wall-associated protein Aap. Our work further documents that Aap binds to glycans exposed on the corneocyte surface, which are commonly exploited by bacteria to facilitate adherence to host cells. Furthermore, we find that Aap orthologues may be responsible for corneocyte adherence in other staphylococci, including in S. aureus.
format	article
author	Paroma Roy Alexander R. Horswill Paul D. Fey
author_facet	Paroma Roy Alexander R. Horswill Paul D. Fey
author_sort	Paroma Roy
title	Glycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap
title_short	Glycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap
title_full	Glycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap
title_fullStr	Glycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap
title_full_unstemmed	Glycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap
title_sort	glycan-dependent corneocyte adherence of <named-content content-type="genus-species">staphylococcus epidermidis</named-content> mediated by the lectin subdomain of aap
publisher	American Society for Microbiology
publishDate	2021
url	https://doaj.org/article/a7639c5ecae24c0b998eb452d0f159b1
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Glycan-Dependent Corneocyte Adherence of <named-content content-type="genus-species">Staphylococcus epidermidis</named-content> Mediated by the Lectin Subdomain of Aap

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