Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase from the Gram-Positive Bacterial Pathogen A. vaginae , an Immunoevasive Factor that Interacts with the Human C5a Anaphylatoxin

The Gram-positive anaerobic human pathogenic bacterium causes most diagnosed cases of bacterial vaginosis as well as opportunistic infections in immunocompromised patients. In addition to its well-established role in carbohydrate metabolism, D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from an...

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Published inFrontiers in microbiology Vol. 8; p. 541
Main Authors Querol-García, Javier, Fernández, Francisco J, Marin, Ana V, Gómez, Sara, Fullà, Daniel, Melchor-Tafur, Cecilia, Franco-Hidalgo, Virginia, Albertí, Sebastián, Juanhuix, Jordi, Rodríguez de Córdoba, Santiago, Regueiro, José R, Vega, M Cristina
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers Media S.A 10.04.2017
Subjects
Microbiology
GAPDH (glyceraldehyde-3-phosphate dehydrogenase)
x-ray crystallography
immunoevasion
gram-positive pathogen
complement system
anaphylatoxin
C5a
chemoattraction
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Abstract The Gram-positive anaerobic human pathogenic bacterium causes most diagnosed cases of bacterial vaginosis as well as opportunistic infections in immunocompromised patients. In addition to its well-established role in carbohydrate metabolism, D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from and have been reported to act as extracellular virulence factors during streptococcal infections. Here, we report the crystal structure of GAPDH from ( GAPDH) at 2.19 Å resolution. The refined model has a crystallographic of 22.6%. GAPDH is a homotetramer wherein each subunit is bound to a nicotinamide adenine dinucleotide (NAD ) molecule. The GAPDH enzyme fulfills essential glycolytic as well as moonlight (non-glycolytic) functions, both of which might be targets of chemotherapeutic intervention. We report that GAPDH interacts with the human C5a anaphylatoxin and inhibits C5a-specific granulocyte chemotaxis, thereby suggesting the participation of GAPDH in complement-targeted immunoevasion in a context of infection. The availability of high-quality structures of GAPDH and other homologous virulence factors from Gram-positive pathogens is critical for drug discovery programs. In this study, sequence and structural differences between GAPDH and related bacterial and eukaryotic GAPDH enzymes are reported in an effort to understand how to subvert the immunoevasive properties of GAPDH and evaluate the potential of GAPDH as a druggable target.
AbstractList The Gram-positive anaerobic human pathogenic bacterium causes most diagnosed cases of bacterial vaginosis as well as opportunistic infections in immunocompromised patients. In addition to its well-established role in carbohydrate metabolism, D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from and have been reported to act as extracellular virulence factors during streptococcal infections. Here, we report the crystal structure of GAPDH from ( GAPDH) at 2.19 Å resolution. The refined model has a crystallographic of 22.6%. GAPDH is a homotetramer wherein each subunit is bound to a nicotinamide adenine dinucleotide (NAD ) molecule. The GAPDH enzyme fulfills essential glycolytic as well as moonlight (non-glycolytic) functions, both of which might be targets of chemotherapeutic intervention. We report that GAPDH interacts with the human C5a anaphylatoxin and inhibits C5a-specific granulocyte chemotaxis, thereby suggesting the participation of GAPDH in complement-targeted immunoevasion in a context of infection. The availability of high-quality structures of GAPDH and other homologous virulence factors from Gram-positive pathogens is critical for drug discovery programs. In this study, sequence and structural differences between GAPDH and related bacterial and eukaryotic GAPDH enzymes are reported in an effort to understand how to subvert the immunoevasive properties of GAPDH and evaluate the potential of GAPDH as a druggable target.
The Gram-positive anaerobic human pathogenic bacterium Atopobium vaginae causes most diagnosed cases of bacterial vaginosis as well as opportunistic infections in immunocompromised patients. In addition to its well-established role in carbohydrate metabolism, D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Streptococcus pyogenes and S. pneumoniae have been reported to act as extracellular virulence factors during streptococcal infections. Here, we report the crystal structure of GAPDH from A. vaginae ( Av GAPDH) at 2.19 Å resolution. The refined model has a crystallographic R free of 22.6%. Av GAPDH is a homotetramer wherein each subunit is bound to a nicotinamide adenine dinucleotide (NAD + ) molecule. The Av GAPDH enzyme fulfills essential glycolytic as well as moonlight (non-glycolytic) functions, both of which might be targets of chemotherapeutic intervention. We report that Av GAPDH interacts in vitro with the human C5a anaphylatoxin and inhibits C5a-specific granulocyte chemotaxis, thereby suggesting the participation of Av GAPDH in complement-targeted immunoevasion in a context of infection. The availability of high-quality structures of Av GAPDH and other homologous virulence factors from Gram-positive pathogens is critical for drug discovery programs. In this study, sequence and structural differences between Av GAPDH and related bacterial and eukaryotic GAPDH enzymes are reported in an effort to understand how to subvert the immunoevasive properties of GAPDH and evaluate the potential of Av GAPDH as a druggable target.
Author Melchor-Tafur, Cecilia
Marin, Ana V
Gómez, Sara
Rodríguez de Córdoba, Santiago
Regueiro, José R
Vega, M Cristina
Querol-García, Javier
Fernández, Francisco J
Juanhuix, Jordi
Franco-Hidalgo, Virginia
Fullà, Daniel
Albertí, Sebastián
AuthorAffiliation 1 Integrated Protein Science for Biomedicine & Biotechnology and Ciber de Enfermedades Raras, Center for Biological Research (CIB-CSIC) Madrid, Spain
2 Department of Immunology, Complutense University School of Medicine Madrid, Spain
4 Abvance Biotech srl Madrid, Spain
5 ALBA Synchrotron, Cerdanyola del Vallès Catalonia, Spain
6 IUNICS, University of the Balearic Islands Palma de Mallorca, Spain
3 Hospital 12 de Octubre Health Research Institute Madrid, Spain
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– name: 6 IUNICS, University of the Balearic Islands Palma de Mallorca, Spain
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  fullname: Juanhuix, Jordi
  organization: ALBA Synchrotron, Cerdanyola del VallèsCatalonia, Spain
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  givenname: Santiago
  surname: Rodríguez de Córdoba
  fullname: Rodríguez de Córdoba, Santiago
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  surname: Regueiro
  fullname: Regueiro, José R
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  givenname: M Cristina
  surname: Vega
  fullname: Vega, M Cristina
  organization: Integrated Protein Science for Biomedicine & Biotechnology and Ciber de Enfermedades Raras, Center for Biological Research (CIB-CSIC)Madrid, Spain
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Copyright Copyright © 2017 Querol-García, Fernández, Marin, Gómez, Fullà, Melchor-Tafur, Franco-Hidalgo, Albertí, Juanhuix, Rodríguez de Córdoba, Regueiro and Vega. 2017 Querol-García, Fernández, Marin, Gómez, Fullà, Melchor-Tafur, Franco-Hidalgo, Albertí, Juanhuix, Rodríguez de Córdoba, Regueiro and Vega
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Keywords GAPDH (glyceraldehyde-3-phosphate dehydrogenase)
x-ray crystallography
immunoevasion
gram-positive pathogen
complement system
anaphylatoxin
C5a
chemoattraction
Language English
License This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
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This article was submitted to Microbial Immunology, a section of the journal Frontiers in Microbiology
Reviewed by: Lubka T. Roumenina, Cordeliers Research Center (INSERM), France; Deborah Schechtman, University of São Paulo, Brazil
These authors have contributed equally to this work.
Edited by: Juarez Antonio Simões Quaresma, Federal University of Pará, Brazil
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Snippet The Gram-positive anaerobic human pathogenic bacterium causes most diagnosed cases of bacterial vaginosis as well as opportunistic infections in...
The Gram-positive anaerobic human pathogenic bacterium Atopobium vaginae causes most diagnosed cases of bacterial vaginosis as well as opportunistic infections...
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Title Crystal Structure of Glyceraldehyde-3-Phosphate Dehydrogenase from the Gram-Positive Bacterial Pathogen A. vaginae , an Immunoevasive Factor that Interacts with the Human C5a Anaphylatoxin
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