Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/51511

TitleAbility of phages to infect Acinetobacter calcoaceticus-Acinetobacter baumannii complex species through acquisition of different pectate lyase depolymerase domains
Author(s)Oliveira, Hugo
Costa, Ana Rita
Konstantinidis, Nico
Ferreira, A.
Akturk, Ergun
Sillankorva, Sanna
Nemec, Alexander
Shneider, Mikhail
Dötsch, Andreas
Azeredo, Joana
KeywordsAcinetobacter calcoaceticus-Acinetobacter baumannii complex
bacteriophage
comparative genomics
depolymerase
capsule
Issue dateDec-2017
PublisherWiley-Blackwell
JournalEnvironmental Microbiology
CitationOliveira, Hugo; Costa, Ana Rita; Konstantinidis, Nico; Ferreira, A.; Akturk, Ergun; Sillankorva, Sanna; Nemec, Alexander; Shneider, Mikhail; Dötsch, Andreas; Azeredo, Joana, Ability of phages to infect Acinetobacter calcoaceticus-Acinetobacter baumannii complex species through acquisition of different pectate lyase depolymerase domains. Environmental Microbiology, 19(12), 5060-5077, 2017
Abstract(s)Bacteriophages are ubiquitous in nature and represent a vast repository of genetic diversity, which is driven by the endless coevolution cycle with a diversified group of bacterial hosts. Studying phage-host interactions is important to gain novel insights into their dynamic adaptation. In this study, we isolated 12 phages infecting species of the Acinetobacter baumannii-Acinetobacter calcoaceticus complex which exhibited a narrow host range and similar morphological features (podoviruses with short tails of 9-12 nm and isometric heads of 50-60 nm). Notably, the alignment of the newly sequenced phage genomes (40-41 kb of DNA length) and all Acinetobacter podoviruses deposited in Genbank has shown high synteny, regardless of the date and source of isolation that spans from America to Europe and Asia. Interestingly, the C-terminal pectate lyase domain of these phage tail fibers is often the only difference found among these viral genomes, demonstrating a very specific genomic variation during the course of their evolution. We proved that the pectate lyase domain is responsible for phage depolymerase activity and binding to specific Acinetobacter bacterial capsules. We discuss how this mechanism of phage-host co-evolution impacts the tail specificity apparatus of Acinetobacter podoviruses.
TypeArticle
URIhttp://hdl.handle.net/1822/51511
DOI10.1111/1462-2920.13970
ISSN1462-2912
e-ISSN1462-2920
Publisher versionhttp://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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