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Possible Roles of Ectophosphatases in Host-Parasite Interactions
The interaction and survival of pathogens in hostile environments and in confrontation with host immune responses are important mechanisms for the establishment of infection. Ectophosphatases are enzymes localized at the plasma membrane of cells, and their active sites face the external medium rathe...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3095255/ https://www.ncbi.nlm.nih.gov/pubmed/21603194 http://dx.doi.org/10.1155/2011/479146 |
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author | Gomes, Marta T. Lopes, Angela H. Meyer-Fernandes, José Roberto |
author_facet | Gomes, Marta T. Lopes, Angela H. Meyer-Fernandes, José Roberto |
author_sort | Gomes, Marta T. |
collection | PubMed |
description | The interaction and survival of pathogens in hostile environments and in confrontation with host immune responses are important mechanisms for the establishment of infection. Ectophosphatases are enzymes localized at the plasma membrane of cells, and their active sites face the external medium rather than the cytoplasm. Once activated, these enzymes are able to hydrolyze phosphorylated substrates in the extracellular milieu. Several studies demonstrated the presence of surface-located ecto-phosphatases in a vast number of pathogenic organisms, including bacteria, protozoa, and fungi. Little is known about the role of ecto-phosphatases in host-pathogen interactions. The present paper provides an overview of recent findings related to the virulence induced by these surface molecules in protozoa and fungi. |
format | Text |
id | pubmed-3095255 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-30952552011-05-20 Possible Roles of Ectophosphatases in Host-Parasite Interactions Gomes, Marta T. Lopes, Angela H. Meyer-Fernandes, José Roberto J Parasitol Res Review Article The interaction and survival of pathogens in hostile environments and in confrontation with host immune responses are important mechanisms for the establishment of infection. Ectophosphatases are enzymes localized at the plasma membrane of cells, and their active sites face the external medium rather than the cytoplasm. Once activated, these enzymes are able to hydrolyze phosphorylated substrates in the extracellular milieu. Several studies demonstrated the presence of surface-located ecto-phosphatases in a vast number of pathogenic organisms, including bacteria, protozoa, and fungi. Little is known about the role of ecto-phosphatases in host-pathogen interactions. The present paper provides an overview of recent findings related to the virulence induced by these surface molecules in protozoa and fungi. Hindawi Publishing Corporation 2011 2011-04-26 /pmc/articles/PMC3095255/ /pubmed/21603194 http://dx.doi.org/10.1155/2011/479146 Text en Copyright © 2011 Marta T. Gomes et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Gomes, Marta T. Lopes, Angela H. Meyer-Fernandes, José Roberto Possible Roles of Ectophosphatases in Host-Parasite Interactions |
title | Possible Roles of Ectophosphatases in Host-Parasite Interactions |
title_full | Possible Roles of Ectophosphatases in Host-Parasite Interactions |
title_fullStr | Possible Roles of Ectophosphatases in Host-Parasite Interactions |
title_full_unstemmed | Possible Roles of Ectophosphatases in Host-Parasite Interactions |
title_short | Possible Roles of Ectophosphatases in Host-Parasite Interactions |
title_sort | possible roles of ectophosphatases in host-parasite interactions |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3095255/ https://www.ncbi.nlm.nih.gov/pubmed/21603194 http://dx.doi.org/10.1155/2011/479146 |
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