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Schistosoma-associated Salmonella resist antibiotics via specific fimbrial attachments to the flatworm
BACKGROUND: Schistosomes are parasitic helminths that infect humans through dermo-invasion while in contaminated water. Salmonella are also a common water-borne human pathogen that infects the gastrointestinal tract via the oral route. Both pathogens eventually enter the systemic circulation as part...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3143092/ https://www.ncbi.nlm.nih.gov/pubmed/21711539 http://dx.doi.org/10.1186/1756-3305-4-123 |
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author | Barnhill, Alison E Novozhilova, Ekaterina Day, Tim A Carlson, Steve A |
author_facet | Barnhill, Alison E Novozhilova, Ekaterina Day, Tim A Carlson, Steve A |
author_sort | Barnhill, Alison E |
collection | PubMed |
description | BACKGROUND: Schistosomes are parasitic helminths that infect humans through dermo-invasion while in contaminated water. Salmonella are also a common water-borne human pathogen that infects the gastrointestinal tract via the oral route. Both pathogens eventually enter the systemic circulation as part of their respective disease processes. Concurrent Schistosoma-Salmonella infections are common and are complicated by the bacteria adhering to adult schistosomes present in the mesenteric vasculature. This interaction provides a refuge in which the bacterium can putatively evade antibiotic therapy and anthelmintic monotherapy can lead to a massive release of occult Salmonella. RESULTS: Using a novel antibiotic protection assay, our results reveal that Schistosoma-associated Salmonella are refractory to eight different antibiotics commonly used to treat salmonellosis. The efficacy of these antibiotics was decreased by a factor of 4 to 16 due to this association. Salmonella binding to schistosomes occurs via a specific fimbrial protein (FimH) present on the surface on the bacterium. This same fimbrial protein confers the ability of Salmonella to bind to mammalian cells. CONCLUSIONS: Salmonella can evade certain antibiotics by binding to Schistosoma. As a result, effective bactericidal concentrations of antibiotics are unfortunately above the achievable therapeutic levels of the drugs in co-infected individuals. Salmonella-Schistosoma binding is analogous to the adherence of Salmonella to cells lining the mammalian intestine. Perturbing this binding is the key to eliminating Salmonella that complicate schistosomiasis. |
format | Online Article Text |
id | pubmed-3143092 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-31430922011-07-26 Schistosoma-associated Salmonella resist antibiotics via specific fimbrial attachments to the flatworm Barnhill, Alison E Novozhilova, Ekaterina Day, Tim A Carlson, Steve A Parasit Vectors Research BACKGROUND: Schistosomes are parasitic helminths that infect humans through dermo-invasion while in contaminated water. Salmonella are also a common water-borne human pathogen that infects the gastrointestinal tract via the oral route. Both pathogens eventually enter the systemic circulation as part of their respective disease processes. Concurrent Schistosoma-Salmonella infections are common and are complicated by the bacteria adhering to adult schistosomes present in the mesenteric vasculature. This interaction provides a refuge in which the bacterium can putatively evade antibiotic therapy and anthelmintic monotherapy can lead to a massive release of occult Salmonella. RESULTS: Using a novel antibiotic protection assay, our results reveal that Schistosoma-associated Salmonella are refractory to eight different antibiotics commonly used to treat salmonellosis. The efficacy of these antibiotics was decreased by a factor of 4 to 16 due to this association. Salmonella binding to schistosomes occurs via a specific fimbrial protein (FimH) present on the surface on the bacterium. This same fimbrial protein confers the ability of Salmonella to bind to mammalian cells. CONCLUSIONS: Salmonella can evade certain antibiotics by binding to Schistosoma. As a result, effective bactericidal concentrations of antibiotics are unfortunately above the achievable therapeutic levels of the drugs in co-infected individuals. Salmonella-Schistosoma binding is analogous to the adherence of Salmonella to cells lining the mammalian intestine. Perturbing this binding is the key to eliminating Salmonella that complicate schistosomiasis. BioMed Central 2011-06-28 /pmc/articles/PMC3143092/ /pubmed/21711539 http://dx.doi.org/10.1186/1756-3305-4-123 Text en Copyright ©2011 Barnhill et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Barnhill, Alison E Novozhilova, Ekaterina Day, Tim A Carlson, Steve A Schistosoma-associated Salmonella resist antibiotics via specific fimbrial attachments to the flatworm |
title | Schistosoma-associated Salmonella resist antibiotics via specific fimbrial attachments to the flatworm |
title_full | Schistosoma-associated Salmonella resist antibiotics via specific fimbrial attachments to the flatworm |
title_fullStr | Schistosoma-associated Salmonella resist antibiotics via specific fimbrial attachments to the flatworm |
title_full_unstemmed | Schistosoma-associated Salmonella resist antibiotics via specific fimbrial attachments to the flatworm |
title_short | Schistosoma-associated Salmonella resist antibiotics via specific fimbrial attachments to the flatworm |
title_sort | schistosoma-associated salmonella resist antibiotics via specific fimbrial attachments to the flatworm |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3143092/ https://www.ncbi.nlm.nih.gov/pubmed/21711539 http://dx.doi.org/10.1186/1756-3305-4-123 |
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