Unpuzzling friunavirus-host interactions one piece at a time: phage recognizes Acinetobacter pittii via a new K38 capsule depolymerase

Detalhes bibliográficos
Autor(a) principal: Domingues, Rita
Data de Publicação: 2021
Outros Autores: Barbosa, Ana Teresa Moutinho, Santos, Sílvio Roberto Branco, Pires, Diana Priscila Penso, Save, Jonathan, Resch, Grégory, Azeredo, Joana, Oliveira, Hugo Alexandre Mendes
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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spelling 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 reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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