Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | https://hdl.handle.net/10216/82047 |
Resumo: | Mycobacterium avium causes respiratory disease in susceptible individuals, as well as disseminated infections in immunocompromised hosts, being an important cause of morbidity and mortality among these populations. Current therapies consist of a combination of antibiotics taken for at least 6 months, with no more than 60% overall clinical success. Furthermore, mycobacterial antibiotic resistance is increasing worldwide, urging the need to develop novel classes of antimicrobial drugs. One potential and interesting alternative strategy is the use of antimicrobial peptides (AMP). These are present in almost all living organisms as part of their immune system, acting as a first barrier against invading pathogens. In this context, we investigated the effect of several lactoferrin-derived AMP against M. avium. Short peptide sequences from both human and bovine lactoferricins, namely, hLFcin1-11 and LFcin17-30, as well as variants obtained by specific amino acid substitutions, were evaluated. All tested peptides significantly inhibited the axenic growth of M. avium, the bovine peptides being more active than the human. Arginine residues were found to be crucial for the display of antimycobacterial activity, whereas the all-D-amino-acid analogue of the bovine sequence displayed the highest mycobactericidal activity. These findings reveal the promising potential of lactoferricins against mycobacteria, thus opening the way for further research on their development and use as a new weapon against mycobacterial infections. |
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Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing MoleculesMedicina básicaBasic medicineMycobacterium avium causes respiratory disease in susceptible individuals, as well as disseminated infections in immunocompromised hosts, being an important cause of morbidity and mortality among these populations. Current therapies consist of a combination of antibiotics taken for at least 6 months, with no more than 60% overall clinical success. Furthermore, mycobacterial antibiotic resistance is increasing worldwide, urging the need to develop novel classes of antimicrobial drugs. One potential and interesting alternative strategy is the use of antimicrobial peptides (AMP). These are present in almost all living organisms as part of their immune system, acting as a first barrier against invading pathogens. In this context, we investigated the effect of several lactoferrin-derived AMP against M. avium. Short peptide sequences from both human and bovine lactoferricins, namely, hLFcin1-11 and LFcin17-30, as well as variants obtained by specific amino acid substitutions, were evaluated. All tested peptides significantly inhibited the axenic growth of M. avium, the bovine peptides being more active than the human. Arginine residues were found to be crucial for the display of antimycobacterial activity, whereas the all-D-amino-acid analogue of the bovine sequence displayed the highest mycobactericidal activity. These findings reveal the promising potential of lactoferricins against mycobacteria, thus opening the way for further research on their development and use as a new weapon against mycobacterial infections.20142014-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10216/82047eng0066-480410.1128/aac.02728-13Tania SilvaBarbara MagalhaesSilvia MaiaPaula GomesKamran NazmiJan G M BolscherPedro N RodriguesMargarida BastosMaria Salome Gomesinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-29T13:42:47Zoai:repositorio-aberto.up.pt:10216/82047Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T23:46:21.661708Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules |
title |
Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules |
spellingShingle |
Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules Tania Silva Medicina básica Basic medicine |
title_short |
Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules |
title_full |
Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules |
title_fullStr |
Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules |
title_full_unstemmed |
Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules |
title_sort |
Killing of Mycobacterium avium by Lactoferricin Peptides: Improved Activity of Arginine- and D-Amino-Acid-Containing Molecules |
author |
Tania Silva |
author_facet |
Tania Silva Barbara Magalhaes Silvia Maia Paula Gomes Kamran Nazmi Jan G M Bolscher Pedro N Rodrigues Margarida Bastos Maria Salome Gomes |
author_role |
author |
author2 |
Barbara Magalhaes Silvia Maia Paula Gomes Kamran Nazmi Jan G M Bolscher Pedro N Rodrigues Margarida Bastos Maria Salome Gomes |
author2_role |
author author author author author author author author |
dc.contributor.author.fl_str_mv |
Tania Silva Barbara Magalhaes Silvia Maia Paula Gomes Kamran Nazmi Jan G M Bolscher Pedro N Rodrigues Margarida Bastos Maria Salome Gomes |
dc.subject.por.fl_str_mv |
Medicina básica Basic medicine |
topic |
Medicina básica Basic medicine |
description |
Mycobacterium avium causes respiratory disease in susceptible individuals, as well as disseminated infections in immunocompromised hosts, being an important cause of morbidity and mortality among these populations. Current therapies consist of a combination of antibiotics taken for at least 6 months, with no more than 60% overall clinical success. Furthermore, mycobacterial antibiotic resistance is increasing worldwide, urging the need to develop novel classes of antimicrobial drugs. One potential and interesting alternative strategy is the use of antimicrobial peptides (AMP). These are present in almost all living organisms as part of their immune system, acting as a first barrier against invading pathogens. In this context, we investigated the effect of several lactoferrin-derived AMP against M. avium. Short peptide sequences from both human and bovine lactoferricins, namely, hLFcin1-11 and LFcin17-30, as well as variants obtained by specific amino acid substitutions, were evaluated. All tested peptides significantly inhibited the axenic growth of M. avium, the bovine peptides being more active than the human. Arginine residues were found to be crucial for the display of antimycobacterial activity, whereas the all-D-amino-acid analogue of the bovine sequence displayed the highest mycobactericidal activity. These findings reveal the promising potential of lactoferricins against mycobacteria, thus opening the way for further research on their development and use as a new weapon against mycobacterial infections. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014 2014-01-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://hdl.handle.net/10216/82047 |
url |
https://hdl.handle.net/10216/82047 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0066-4804 10.1128/aac.02728-13 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799135780813144065 |