Cargando…
The Enolase of the Haemophilus influenzae Mediates Binding to Collagens: An Extracellular Matrix Component
Enolase proteins play a significant role as moonlighting proteins. In their role as surface-associated enolase, they have multiple functions as they interact with extracellular matrix proteins. Type I and III collagens are the major constituents of this extracellular matrix, and collagen is one of t...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10650631/ https://www.ncbi.nlm.nih.gov/pubmed/37958487 http://dx.doi.org/10.3390/ijms242115499 |
_version_ | 1785135824999809024 |
---|---|
author | Osorio-Aguilar, Yesenia Gonzalez-Vazquez, Maria Cristina Lozano-Zarain, Patricia Martinez-Laguna, Ygnacio Baylon-Pacheco, Lidia Rosales-Encina, Jose Luis Carabarin-Lima, Alejandro Rocha-Gracia, Rosa del Carmen |
author_facet | Osorio-Aguilar, Yesenia Gonzalez-Vazquez, Maria Cristina Lozano-Zarain, Patricia Martinez-Laguna, Ygnacio Baylon-Pacheco, Lidia Rosales-Encina, Jose Luis Carabarin-Lima, Alejandro Rocha-Gracia, Rosa del Carmen |
author_sort | Osorio-Aguilar, Yesenia |
collection | PubMed |
description | Enolase proteins play a significant role as moonlighting proteins. In their role as surface-associated enolase, they have multiple functions as they interact with extracellular matrix proteins. Type I and III collagens are the major constituents of this extracellular matrix, and collagen is one of the targets of interaction with the enolase of many pathogens, thereby helping the colonization process and promoting the subsequent invasion of the host. This work aimed to determine the participation of non-typeable H. influenzae enolase as a collagen-binding protein. In this study, through the use of in vitro tests it was demonstrated that recombinant enolase of non-typeable H. influenzae (rNTHiENO) strongly binds to type I collagen. Using molecular docking, the residues that could take part in the interaction of non-typeable H. influenzae enolase-type I collagen (NTHiENO-Cln I) and non-typeable H. influenzae enolase-type III collagen (NTHiENO-Cln III) were identified. However, in vitro assays show that NTHiENO has a better affinity to interact with Cln I, concerning type Cln III. The interaction of NTHiENO with collagen could play a significant role in the colonization process; this would allow H. influenzae to increase its virulence factors and strengthen its pathogenesis. |
format | Online Article Text |
id | pubmed-10650631 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106506312023-10-24 The Enolase of the Haemophilus influenzae Mediates Binding to Collagens: An Extracellular Matrix Component Osorio-Aguilar, Yesenia Gonzalez-Vazquez, Maria Cristina Lozano-Zarain, Patricia Martinez-Laguna, Ygnacio Baylon-Pacheco, Lidia Rosales-Encina, Jose Luis Carabarin-Lima, Alejandro Rocha-Gracia, Rosa del Carmen Int J Mol Sci Article Enolase proteins play a significant role as moonlighting proteins. In their role as surface-associated enolase, they have multiple functions as they interact with extracellular matrix proteins. Type I and III collagens are the major constituents of this extracellular matrix, and collagen is one of the targets of interaction with the enolase of many pathogens, thereby helping the colonization process and promoting the subsequent invasion of the host. This work aimed to determine the participation of non-typeable H. influenzae enolase as a collagen-binding protein. In this study, through the use of in vitro tests it was demonstrated that recombinant enolase of non-typeable H. influenzae (rNTHiENO) strongly binds to type I collagen. Using molecular docking, the residues that could take part in the interaction of non-typeable H. influenzae enolase-type I collagen (NTHiENO-Cln I) and non-typeable H. influenzae enolase-type III collagen (NTHiENO-Cln III) were identified. However, in vitro assays show that NTHiENO has a better affinity to interact with Cln I, concerning type Cln III. The interaction of NTHiENO with collagen could play a significant role in the colonization process; this would allow H. influenzae to increase its virulence factors and strengthen its pathogenesis. MDPI 2023-10-24 /pmc/articles/PMC10650631/ /pubmed/37958487 http://dx.doi.org/10.3390/ijms242115499 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Osorio-Aguilar, Yesenia Gonzalez-Vazquez, Maria Cristina Lozano-Zarain, Patricia Martinez-Laguna, Ygnacio Baylon-Pacheco, Lidia Rosales-Encina, Jose Luis Carabarin-Lima, Alejandro Rocha-Gracia, Rosa del Carmen The Enolase of the Haemophilus influenzae Mediates Binding to Collagens: An Extracellular Matrix Component |
title | The Enolase of the Haemophilus influenzae Mediates Binding to Collagens: An Extracellular Matrix Component |
title_full | The Enolase of the Haemophilus influenzae Mediates Binding to Collagens: An Extracellular Matrix Component |
title_fullStr | The Enolase of the Haemophilus influenzae Mediates Binding to Collagens: An Extracellular Matrix Component |
title_full_unstemmed | The Enolase of the Haemophilus influenzae Mediates Binding to Collagens: An Extracellular Matrix Component |
title_short | The Enolase of the Haemophilus influenzae Mediates Binding to Collagens: An Extracellular Matrix Component |
title_sort | enolase of the haemophilus influenzae mediates binding to collagens: an extracellular matrix component |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10650631/ https://www.ncbi.nlm.nih.gov/pubmed/37958487 http://dx.doi.org/10.3390/ijms242115499 |
work_keys_str_mv | AT osorioaguilaryesenia theenolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT gonzalezvazquezmariacristina theenolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT lozanozarainpatricia theenolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT martinezlagunaygnacio theenolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT baylonpachecolidia theenolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT rosalesencinajoseluis theenolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT carabarinlimaalejandro theenolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT rochagraciarosadelcarmen theenolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT osorioaguilaryesenia enolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT gonzalezvazquezmariacristina enolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT lozanozarainpatricia enolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT martinezlagunaygnacio enolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT baylonpachecolidia enolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT rosalesencinajoseluis enolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT carabarinlimaalejandro enolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent AT rochagraciarosadelcarmen enolaseofthehaemophilusinfluenzaemediatesbindingtocollagensanextracellularmatrixcomponent |