Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/74589 |
Resumo: | Acinetobacter pittii is a species that belong to the Acinetobacter calcoaceticus-baumannii complex, increasingly recognized as major nosocomial bacterial pathogens, often associated with multiple drug-resistances. The capsule surrounding the bacteria represents a main virulence factor, helping cells avoid phage predation and host immunity. Accordingly, a better understanding of the phage infection mechanisms is required to efficiently develop phage therapy against Acinetobacter of different capsular types. Here, we report the isolation of the novel A. pittii-infecting Fri1-like phage vB_Api_3043-K38 (3043-K38) of the Podoviridae morphotype, from sewage samples. Its 41,580 bp linear double-stranded DNA genome harbours 53 open reading frames and 302 bp of terminal repeats. We show that all studied Acinetobacter Fri1-like viruses have highly similar genomes, which differentiate only at the genes coding for tailspike, likely to adapt to different host receptors. The isolated phage 3043-K38 specifically recognizes an untapped Acinetobacter K38 capsule type via a novel tailspike with K38 depolymerase activity. The recombinant K38 depolymerase region of the tailspike (center-end region) forms a thermostable trimer, and quickly degrades capsules. When the K38 depolymerase is applied to the cells, it makes them resistant to phage predation. Interestingly, while K38 depolymerase treatments do not synergize with antibiotics, it makes bacterial cells highly susceptible to the host serum complement. In summary, we characterized a novel phage-encoded K38 depolymerase, which not only advances our understanding of phage-host interactions, but could also be further explored as a new antibacterial agent against drug-resistant Acinetobacter. |
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Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymeraseAcinetobacter baumanniiBacteriophageTailspikeDepolymeraseAnti-virulenceCapsuleScience & TechnologyAcinetobacter pittii is a species that belong to the Acinetobacter calcoaceticus-baumannii complex, increasingly recognized as major nosocomial bacterial pathogens, often associated with multiple drug-resistances. The capsule surrounding the bacteria represents a main virulence factor, helping cells avoid phage predation and host immunity. Accordingly, a better understanding of the phage infection mechanisms is required to efficiently develop phage therapy against Acinetobacter of different capsular types. Here, we report the isolation of the novel A. pittii-infecting Fri1-like phage vB_Api_3043-K38 (3043-K38) of the Podoviridae morphotype, from sewage samples. Its 41,580 bp linear double-stranded DNA genome harbours 53 open reading frames and 302 bp of terminal repeats. We show that all studied Acinetobacter Fri1-like viruses have highly similar genomes, which differentiate only at the genes coding for tailspike, likely to adapt to different host receptors. The isolated phage 3043-K38 specifically recognizes an untapped Acinetobacter K38 capsule type via a novel tailspike with K38 depolymerase activity. The recombinant K38 depolymerase region of the tailspike (center-end region) forms a thermostable trimer, and quickly degrades capsules. When the K38 depolymerase is applied to the cells, it makes them resistant to phage predation. Interestingly, while K38 depolymerase treatments do not synergize with antibiotics, it makes bacterial cells highly susceptible to the host serum complement. In summary, we characterized a novel phage-encoded K38 depolymerase, which not only advances our understanding of phage-host interactions, but could also be further explored as a new antibacterial agent against drug-resistant Acinetobacter.This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UIDB/04469/2020 unit. This project has been also funded by a Research Grant 2020 of the European Society of Clinical Microbiology and Infectious Diseases (ESCMID) to H.O.info:eu-repo/semantics/publishedVersionMDPIUniversidade do MinhoDomingues, RitaBarbosa, Ana Teresa MoutinhoSantos, Sílvio Roberto BrancoPires, Diana Priscila PensoSave, JonathanResch, GrégoryAzeredo, JoanaOliveira, Hugo Alexandre Mendes2021-10-262021-10-26T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/74589engDomingues, Rita; Barbosa, Ana; Santos, Sílvio Roberto Branco; Pires, Diana P.; Save, Jonathan; Resch, Grégory; Azeredo, Joana; Oliveira, Hugo, Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase. Antibiotics, 10(11), 1304, 20212079-638210.3390/antibiotics10111304https://www.mdpi.com/2079-6382/10/11/1304info: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:RCAAP2023-07-21T12:47:20Zoai:repositorium.sdum.uminho.pt:1822/74589Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:45:26.814528Repositório 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 |
Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase |
title |
Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase |
spellingShingle |
Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase Domingues, Rita Acinetobacter baumannii Bacteriophage Tailspike Depolymerase Anti-virulence Capsule Science & Technology |
title_short |
Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase |
title_full |
Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase |
title_fullStr |
Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase |
title_full_unstemmed |
Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase |
title_sort |
Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase |
author |
Domingues, Rita |
author_facet |
Domingues, Rita Barbosa, Ana Teresa Moutinho Santos, Sílvio Roberto Branco Pires, Diana Priscila Penso Save, Jonathan Resch, Grégory Azeredo, Joana Oliveira, Hugo Alexandre Mendes |
author_role |
author |
author2 |
Barbosa, Ana Teresa Moutinho Santos, Sílvio Roberto Branco Pires, Diana Priscila Penso Save, Jonathan Resch, Grégory Azeredo, Joana Oliveira, Hugo Alexandre Mendes |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Domingues, Rita Barbosa, Ana Teresa Moutinho Santos, Sílvio Roberto Branco Pires, Diana Priscila Penso Save, Jonathan Resch, Grégory Azeredo, Joana Oliveira, Hugo Alexandre Mendes |
dc.subject.por.fl_str_mv |
Acinetobacter baumannii Bacteriophage Tailspike Depolymerase Anti-virulence Capsule Science & Technology |
topic |
Acinetobacter baumannii Bacteriophage Tailspike Depolymerase Anti-virulence Capsule Science & Technology |
description |
Acinetobacter pittii is a species that belong to the Acinetobacter calcoaceticus-baumannii complex, increasingly recognized as major nosocomial bacterial pathogens, often associated with multiple drug-resistances. The capsule surrounding the bacteria represents a main virulence factor, helping cells avoid phage predation and host immunity. Accordingly, a better understanding of the phage infection mechanisms is required to efficiently develop phage therapy against Acinetobacter of different capsular types. Here, we report the isolation of the novel A. pittii-infecting Fri1-like phage vB_Api_3043-K38 (3043-K38) of the Podoviridae morphotype, from sewage samples. Its 41,580 bp linear double-stranded DNA genome harbours 53 open reading frames and 302 bp of terminal repeats. We show that all studied Acinetobacter Fri1-like viruses have highly similar genomes, which differentiate only at the genes coding for tailspike, likely to adapt to different host receptors. The isolated phage 3043-K38 specifically recognizes an untapped Acinetobacter K38 capsule type via a novel tailspike with K38 depolymerase activity. The recombinant K38 depolymerase region of the tailspike (center-end region) forms a thermostable trimer, and quickly degrades capsules. When the K38 depolymerase is applied to the cells, it makes them resistant to phage predation. Interestingly, while K38 depolymerase treatments do not synergize with antibiotics, it makes bacterial cells highly susceptible to the host serum complement. In summary, we characterized a novel phage-encoded K38 depolymerase, which not only advances our understanding of phage-host interactions, but could also be further explored as a new antibacterial agent against drug-resistant Acinetobacter. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-10-26 2021-10-26T00:00:00Z |
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 |
http://hdl.handle.net/1822/74589 |
url |
http://hdl.handle.net/1822/74589 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Domingues, Rita; Barbosa, Ana; Santos, Sílvio Roberto Branco; Pires, Diana P.; Save, Jonathan; Resch, Grégory; Azeredo, Joana; Oliveira, Hugo, Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase. Antibiotics, 10(11), 1304, 2021 2079-6382 10.3390/antibiotics10111304 https://www.mdpi.com/2079-6382/10/11/1304 |
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.publisher.none.fl_str_mv |
MDPI |
publisher.none.fl_str_mv |
MDPI |
dc.source.none.fl_str_mv |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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