Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity

Kristian Stødkilde; Jakob Toudahl Nielsen; Steen Vang Petersen; Bernhard Paetzold; Holger Brüggemann; Frans A.A. Mulder; Christian Brix Folsted Andersen

doi:10.3389/fcimb.2022.803004

Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity

Kristian Stødkilde, Jakob Toudahl Nielsen, Steen Vang Petersen, Bernhard Paetzold, Holger Brüggemann, Frans A.A. Mulder, Christian Brix Folsted Andersen^*

^*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

4 Citations (Scopus)

Abstract

Cutibacterium acnes is a predominant bacterium on human skin and is generally regarded as commensal. Recently, the abundantly secreted protein produced by C. acnes, RoxP, was shown to alleviate radical-induced cell damage, presumably via antioxidant activity, which could potentially be harnessed to fortify skin barrier function. The aim of this study was to determine the structure of RoxP and elucidate the mechanisms behind its antioxidative effect. Here, we present the solution structure of RoxP revealing a compact immunoglobulin-like domain containing a long flexible loop which, in concert with the core domain, forms a positively charged groove that could function as a binding site for cofactors or substrates. Although RoxP shares structural features with cell-adhesion proteins, we show that it does not appear to be responsible for adhesion of C. acnes bacteria to human keratinocytes. We identify two tyrosine-containing stretches located in the flexible loop of RoxP, which appear to be responsible for the antioxidant activity of RoxP.

Original language	English
Article number	803004
Journal	Frontiers in cellular and infection microbiology
Volume	12
Number of pages	11
ISSN	2235-2988
DOIs	https://doi.org/10.3389/fcimb.2022.803004
Publication status	Published - Feb 2022

Keywords

antioxidant
Cutibacterium acnes
immunoglobin-like
nuclear magnetic resonance
RoxP
CRYSTAL-STRUCTURE
GROWTH
SKIN MICROBIOTA
FRAGMENT
PROPIONIBACTERIUM-ACNES

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10.3389/fcimb.2022.803004Licence: CC BY

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title = "Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity",

abstract = "Cutibacterium acnes is a predominant bacterium on human skin and is generally regarded as commensal. Recently, the abundantly secreted protein produced by C. acnes, RoxP, was shown to alleviate radical-induced cell damage, presumably via antioxidant activity, which could potentially be harnessed to fortify skin barrier function. The aim of this study was to determine the structure of RoxP and elucidate the mechanisms behind its antioxidative effect. Here, we present the solution structure of RoxP revealing a compact immunoglobulin-like domain containing a long flexible loop which, in concert with the core domain, forms a positively charged groove that could function as a binding site for cofactors or substrates. Although RoxP shares structural features with cell-adhesion proteins, we show that it does not appear to be responsible for adhesion of C. acnes bacteria to human keratinocytes. We identify two tyrosine-containing stretches located in the flexible loop of RoxP, which appear to be responsible for the antioxidant activity of RoxP.",

keywords = "antioxidant, Cutibacterium acnes, immunoglobin-like, nuclear magnetic resonance, RoxP, CRYSTAL-STRUCTURE, GROWTH, SKIN MICROBIOTA, FRAGMENT, PROPIONIBACTERIUM-ACNES",

author = "Kristian St{\o}dkilde and Nielsen, {Jakob Toudahl} and Petersen, {Steen Vang} and Bernhard Paetzold and Holger Br{\"u}ggemann and Mulder, {Frans A.A.} and Andersen, {Christian Brix Folsted}",

note = "Publisher Copyright: Copyright {\textcopyright} 2022 St{\o}dkilde, Nielsen, Petersen, Paetzold, Br{\"u}ggemann, Mulder and Andersen.",

year = "2022",

month = feb,

doi = "10.3389/fcimb.2022.803004",

language = "English",

volume = "12",

journal = "Frontiers in cellular and infection microbiology",

issn = "2235-2988",

publisher = "Frontiers Media SA",

}

Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity. / Stødkilde, Kristian; Nielsen, Jakob Toudahl; Petersen, Steen Vang et al.
In: Frontiers in cellular and infection microbiology, Vol. 12, 803004, 02.2022.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity

AU - Stødkilde, Kristian

AU - Nielsen, Jakob Toudahl

AU - Petersen, Steen Vang

AU - Paetzold, Bernhard

AU - Brüggemann, Holger

AU - Mulder, Frans A.A.

AU - Andersen, Christian Brix Folsted

PY - 2022/2

Y1 - 2022/2

N2 - Cutibacterium acnes is a predominant bacterium on human skin and is generally regarded as commensal. Recently, the abundantly secreted protein produced by C. acnes, RoxP, was shown to alleviate radical-induced cell damage, presumably via antioxidant activity, which could potentially be harnessed to fortify skin barrier function. The aim of this study was to determine the structure of RoxP and elucidate the mechanisms behind its antioxidative effect. Here, we present the solution structure of RoxP revealing a compact immunoglobulin-like domain containing a long flexible loop which, in concert with the core domain, forms a positively charged groove that could function as a binding site for cofactors or substrates. Although RoxP shares structural features with cell-adhesion proteins, we show that it does not appear to be responsible for adhesion of C. acnes bacteria to human keratinocytes. We identify two tyrosine-containing stretches located in the flexible loop of RoxP, which appear to be responsible for the antioxidant activity of RoxP.

AB - Cutibacterium acnes is a predominant bacterium on human skin and is generally regarded as commensal. Recently, the abundantly secreted protein produced by C. acnes, RoxP, was shown to alleviate radical-induced cell damage, presumably via antioxidant activity, which could potentially be harnessed to fortify skin barrier function. The aim of this study was to determine the structure of RoxP and elucidate the mechanisms behind its antioxidative effect. Here, we present the solution structure of RoxP revealing a compact immunoglobulin-like domain containing a long flexible loop which, in concert with the core domain, forms a positively charged groove that could function as a binding site for cofactors or substrates. Although RoxP shares structural features with cell-adhesion proteins, we show that it does not appear to be responsible for adhesion of C. acnes bacteria to human keratinocytes. We identify two tyrosine-containing stretches located in the flexible loop of RoxP, which appear to be responsible for the antioxidant activity of RoxP.

KW - antioxidant

KW - Cutibacterium acnes

KW - immunoglobin-like

KW - nuclear magnetic resonance

KW - RoxP

KW - CRYSTAL-STRUCTURE

KW - GROWTH

KW - SKIN MICROBIOTA

KW - FRAGMENT

KW - PROPIONIBACTERIUM-ACNES

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U2 - 10.3389/fcimb.2022.803004

DO - 10.3389/fcimb.2022.803004

M3 - Journal article

C2 - 35223541

AN - SCOPUS:85125220602

SN - 2235-2988

VL - 12

JO - Frontiers in cellular and infection microbiology

JF - Frontiers in cellular and infection microbiology

M1 - 803004

ER -

Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity

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