Proteomic Characterization of the Oral Pathogen <i>Filifactor alocis</i> Reveals Key Inter-Protein Interactions of Its RTX Toxin: FtxA

<i>Filifactor alocis</i> is a Gram-positive asaccharolytic, obligate anaerobic rod that has been isolated from a variety of oral infections including periodontitis, peri-implantitis, and odontogenic abscesses. As a newly emerging pathogen, its type strain has been investigated for pathog...

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Main Authors: Kai Bao, Rolf Claesson, Peter Gehrig, Jonas Grossmann, Jan Oscarsson, Georgios N. Belibasakis
Format: Article
Language:English
Published: MDPI AG 2022-05-01
Series:Pathogens
Subjects:
Online Access:https://www.mdpi.com/2076-0817/11/5/590
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author Kai Bao
Rolf Claesson
Peter Gehrig
Jonas Grossmann
Jan Oscarsson
Georgios N. Belibasakis
author_facet Kai Bao
Rolf Claesson
Peter Gehrig
Jonas Grossmann
Jan Oscarsson
Georgios N. Belibasakis
author_sort Kai Bao
collection DOAJ
description <i>Filifactor alocis</i> is a Gram-positive asaccharolytic, obligate anaerobic rod that has been isolated from a variety of oral infections including periodontitis, peri-implantitis, and odontogenic abscesses. As a newly emerging pathogen, its type strain has been investigated for pathogenic properties, yet little is known about its virulence variations among strains. We previously screened the whole genome of nine clinical oral isolates and a reference strain of <i>F. alocis</i>, and they expressed a novel RTX toxin, FtxA. In the present study, we aimed to use label-free quantification proteomics to characterize the full proteome of those ten <i>F. alocis</i> strains. A total of 872 proteins were quantified, and 97 among them were differentially expressed in FtxA-positive strains compared with the negative strains. In addition, 44 of these differentially expressed proteins formed 66 pairs of associations based on their predicted functions, which included clusters of proteins with DNA repair/mediated transformation and catalytic activity-related function, indicating different biosynthetic activities among strains. FtxA displayed specific interactions with another six intracellular proteins, forming a functional cluster that could discriminate between FtxA-producing and non-producing strains. Among them were FtxB and FtxD, predicted to be encoded by the same operon as FtxA. While revealing the broader qualitative and quantitative proteomic landscape of <i>F. alocis</i>, this study also sheds light on the deeper functional inter-relationships of FtxA, thus placing this RTX family member into context as a major virulence factor of this species.
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spelling doaj.art-73b435c1162f4d2eb527fb3eaf2e40622023-11-23T12:33:05ZengMDPI AGPathogens2076-08172022-05-0111559010.3390/pathogens11050590Proteomic Characterization of the Oral Pathogen <i>Filifactor alocis</i> Reveals Key Inter-Protein Interactions of Its RTX Toxin: FtxAKai Bao0Rolf Claesson1Peter Gehrig2Jonas Grossmann3Jan Oscarsson4Georgios N. Belibasakis5Division of Oral Diseases, Department of Dental Medicine, Karolinska Institutet, 14104 Huddinge, SwedenDivision of Oral Microbiology, Department of Odontology, Umeå University, 90187 Umeå, SwedenFunctional Genomics Center Zurich, ETH Zurich and University of Zurich, Winterthurerstrasse 190, 8057 Zurich, SwitzerlandFunctional Genomics Center Zurich, ETH Zurich and University of Zurich, Winterthurerstrasse 190, 8057 Zurich, SwitzerlandDivision of Oral Microbiology, Department of Odontology, Umeå University, 90187 Umeå, SwedenDivision of Oral Diseases, Department of Dental Medicine, Karolinska Institutet, 14104 Huddinge, Sweden<i>Filifactor alocis</i> is a Gram-positive asaccharolytic, obligate anaerobic rod that has been isolated from a variety of oral infections including periodontitis, peri-implantitis, and odontogenic abscesses. As a newly emerging pathogen, its type strain has been investigated for pathogenic properties, yet little is known about its virulence variations among strains. We previously screened the whole genome of nine clinical oral isolates and a reference strain of <i>F. alocis</i>, and they expressed a novel RTX toxin, FtxA. In the present study, we aimed to use label-free quantification proteomics to characterize the full proteome of those ten <i>F. alocis</i> strains. A total of 872 proteins were quantified, and 97 among them were differentially expressed in FtxA-positive strains compared with the negative strains. In addition, 44 of these differentially expressed proteins formed 66 pairs of associations based on their predicted functions, which included clusters of proteins with DNA repair/mediated transformation and catalytic activity-related function, indicating different biosynthetic activities among strains. FtxA displayed specific interactions with another six intracellular proteins, forming a functional cluster that could discriminate between FtxA-producing and non-producing strains. Among them were FtxB and FtxD, predicted to be encoded by the same operon as FtxA. While revealing the broader qualitative and quantitative proteomic landscape of <i>F. alocis</i>, this study also sheds light on the deeper functional inter-relationships of FtxA, thus placing this RTX family member into context as a major virulence factor of this species.https://www.mdpi.com/2076-0817/11/5/590<i>Filifactor alocis</i>label-free quantification proteomicsFtxA
spellingShingle Kai Bao
Rolf Claesson
Peter Gehrig
Jonas Grossmann
Jan Oscarsson
Georgios N. Belibasakis
Proteomic Characterization of the Oral Pathogen <i>Filifactor alocis</i> Reveals Key Inter-Protein Interactions of Its RTX Toxin: FtxA
Pathogens
<i>Filifactor alocis</i>
label-free quantification proteomics
FtxA
title Proteomic Characterization of the Oral Pathogen <i>Filifactor alocis</i> Reveals Key Inter-Protein Interactions of Its RTX Toxin: FtxA
title_full Proteomic Characterization of the Oral Pathogen <i>Filifactor alocis</i> Reveals Key Inter-Protein Interactions of Its RTX Toxin: FtxA
title_fullStr Proteomic Characterization of the Oral Pathogen <i>Filifactor alocis</i> Reveals Key Inter-Protein Interactions of Its RTX Toxin: FtxA
title_full_unstemmed Proteomic Characterization of the Oral Pathogen <i>Filifactor alocis</i> Reveals Key Inter-Protein Interactions of Its RTX Toxin: FtxA
title_short Proteomic Characterization of the Oral Pathogen <i>Filifactor alocis</i> Reveals Key Inter-Protein Interactions of Its RTX Toxin: FtxA
title_sort proteomic characterization of the oral pathogen i filifactor alocis i reveals key inter protein interactions of its rtx toxin ftxa
topic <i>Filifactor alocis</i>
label-free quantification proteomics
FtxA
url https://www.mdpi.com/2076-0817/11/5/590
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